US2023322878A1PendingUtilityA1

Compounds for inducing tissue formation and uses thereof

Assignee: HISTIDE AGPriority: Aug 25, 2015Filed: Jan 10, 2023Published: Oct 12, 2023
Est. expiryAug 25, 2035(~9.1 yrs left)· nominal 20-yr term from priority
Inventors:Omar F. Zouani
C07K 14/51C07K 2299/00A61L 27/227C07K 14/475A61P 11/00A61P 11/06A61P 13/12A61P 15/00A61P 17/14A61P 19/00A61P 19/02A61P 19/06A61P 21/00A61P 21/02A61P 25/00A61P 27/02A61P 29/00A61P 3/04A61P 31/04A61P 31/06A61P 43/00A61P 7/02A61P 7/06A61P 9/00A61P 9/04A61P 9/06A61P 9/10A61P 9/12A61K 8/64A61K 38/16A61Q 5/002A61Q 7/00
47
PatentIndex Score
0
Cited by
0
References
0
Claims

Abstract

The present disclosure provides peptides, or variants or analogs thereof, with between 8 and 30 amino acids, having growth factor receptor-binding capability, wherein the RMSD value of the structure coordinates of said peptide, variant or analog thereof with respect to PEPREF is 2.45 Å (Angstroms) or less.

Claims

exact text as granted — not AI-modified
1 - 100 . (canceled) 
     
     
         101 . A peptide that is up to 30 amino acids in length and that comprises a peptide with four amino acids, PEP1;
 wherein PEP1 is selected from the group consisting of SAIS, NAIS and SPIS,   wherein the RMSD value of the structure coordinates of said peptide or peptidomimetic with respect to PEPREF is 2.45 Å (Angstroms) or less;   and wherein PEPREF is   
       
         
           
                 
                 
                 
                 
                 
                 
                 
                 
                 
               
                     
                 
                   ATOM 
                   511 
                   N 
                   LYS 
                   A 
                   1 
                   −14.570 
                   46.437 
                   27.424 
                 
                   ATOM 
                   512 
                   CA 
                   LYS 
                   A 
                   1 
                   −13.512 
                   45.748 
                   28.151 
                 
                   ATOM 
                   513 
                   C 
                   LYS 
                   A 
                   1 
                   −13.655 
                   44.259 
                   27.884 
                 
                   ATOM 
                   514 
                   O 
                   LYS 
                   A 
                   1 
                   −12.769 
                   43.463 
                   28.197 
                 
                   ATOM 
                   515 
                   CB 
                   LYS 
                   A 
                   1 
                   −13.605 
                   46.029 
                   29.652 
                 
                   ATOM 
                   516 
                   CG 
                   LYS 
                   A 
                   1 
                   −13.640 
                   47.509 
                   29.991 
                 
                   ATOM 
                   517 
                   CD 
                   LYS 
                   A 
                   1 
                   −12.615 
                   48.297 
                   29.183 
                 
                   ATOM 
                   518 
                   CE 
                   LYS 
                   A 
                   1 
                   −12.625 
                   49.768 
                   29.575 
                 
                   ATOM 
                   519 
                   NZ 
                   LYS 
                   A 
                   1 
                   −13.994 
                   50.369 
                   29.497 
                 
                   ATOM 
                   520 
                   N 
                   ILE 
                   A 
                   2 
                   −14.792 
                   43.890 
                   27.309 
                 
                   ATOM 
                   521 
                   CA 
                   ILE 
                   A 
                   2 
                   −15.051 
                   42.499 
                   26.967 
                 
                   ATOM 
                   522 
                   C 
                   ILE 
                   A 
                   2 
                   −14.911 
                   42.370 
                   25.444 
                 
                   ATOM 
                   523 
                   O 
                   ILE 
                   A 
                   2 
                   −15.531 
                   43.125 
                   24.683 
                 
                   ATOM 
                   524 
                   CB 
                   ILE 
                   A 
                   2 
                   −16.466 
                   42.065 
                   27.401 
                 
                   ATOM 
                   525 
                   CG1 
                   ILE 
                   A 
                   2 
                   −16.630 
                   42.238 
                   28.915 
                 
                   ATOM 
                   526 
                   CG2 
                   ILE 
                   A 
                   2 
                   −16.710 
                   40.629 
                   26.985 
                 
                   ATOM 
                   527 
                   CD1 
                   ILE 
                   A 
                   2 
                   −15.631 
                   41.478 
                   29.30 
                 
                   ATOM 
                   528 
                   N 
                   PRO 
                   A 
                   3 
                   −14.085 
                   41.411 
                   24.989 
                 
                   ATOM 
                   529 
                   CA 
                   PRO 
                   A 
                   3 
                   −13.789 
                   41.109 
                   23.588 
                 
                   ATOM 
                   530 
                   C 
                   PRO 
                   A 
                   3 
                   −14.998 
                   40.695 
                   22.768 
                 
                   ATOM 
                   531 
                   O 
                   PRO 
                   A 
                   3 
                   −15.969 
                   40.164 
                   23.305 
                 
                   ATOM 
                   532 
                   CB 
                   PRO 
                   A 
                   3 
                   −12.785 
                   39.968 
                   23.688 
                 
                   ATOM 
                   533 
                   CG 
                   PRO 
                   A 
                   3 
                   −12.156 
                   40.166 
                   25.007 
                 
                   ATOM 
                   534 
                   CD 
                   PRO 
                   A 
                   3 
                   −13.330 
                   40.506 
                   25.867 
                 
                   ATOM 
                   535 
                   N 
                   LYS 
                   A 
                   4 
                   −14.937 
                   40.937 
                   21.463 
                 
                   ATOM 
                   536 
                   CA 
                   LYS 
                   A 
                   4 
                   −16.023 
                   40.529 
                   20.590 
                 
                   ATOM 
                   537 
                   C 
                   LYS 
                   A 
                   4 
                   −15.886 
                   39.015 
                   20.391 
                 
                   ATOM 
                   538 
                   O 
                   LYS 
                   A 
                   4 
                   −14.903 
                   38.415 
                   20.831 
                 
                   ATOM 
                   539 
                   CB 
                   LYS 
                   A 
                   4 
                   −15.926 
                   41.244 
                   19.245 
                 
                   ATOM 
                   540 
                   CG 
                   LYS 
                   A 
                   4 
                   −15.802 
                   42.751 
                   19.355 
                 
                   ATOM 
                   541 
                   CD 
                   LYS 
                   A 
                   4 
                   −16.292 
                   43.433 
                   18.083 
                 
                   ATOM 
                   542 
                   CE 
                   LYS 
                   A 
                   4 
                   −16.162 
                   44.943 
                   18.177 
                 
                   ATOM 
                   543 
                   NZ 
                   LYS 
                   A 
                   4 
                   −16.825 
                   45.628 
                   17.019 
                 
                   ATOM 
                   544 
                   N 
                   ALA 
                   A 
                   5 
                   −16.85 
                   38.393 
                   19.759 
                 
                   ATOM 
                   545 
                   CA 
                   ALA 
                   A 
                   5 
                   −16.811 
                   36.955 
                   19.507 
                 
                   ATOM 
                   546 
                   C 
                   ALA 
                   A 
                   5 
                   −15.772 
                   36.771 
                   18.416 
                 
                   ATOM 
                   547 
                   O 
                   ALA 
                   A 
                   5 
                   −15.727 
                   37.534 
                   17.455 
                 
                   ATOM 
                   548 
                   CB 
                   ALA 
                   A 
                   5 
                   −18.168 
                   36.419 
                   19.043 
                 
                   ATOM 
                   549 
                   N 
                   CYS 
                   A 
                   6 
                   −14.935 
                   35.756 
                   18.562 
                 
                   ATOM 
                   550 
                   CA 
                   CYS 
                   A 
                   6 
                   −13.887 
                   35.518 
                   17.584 
                 
                   ATOM 
                   551 
                   C 
                   CYS 
                   A 
                   6 
                   −14.347 
                   34.765 
                   16.338 
                 
                   ATOM 
                   552 
                   O 
                   CYS 
                   A 
                   6 
                   −15.327 
                   34.018 
                   16.368 
                 
                   ATOM 
                   553 
                   CB 
                   CYS 
                   A 
                   6 
                   −12.743 
                   34.768 
                   18.241 
                 
                   ATOM 
                   554 
                   SG 
                   CYS 
                   A 
                   6 
                   −11.198 
                   34.959 
                   17.353 
                 
                   ATOM 
                   555 
                   N 
                   CYS 
                   A 
                   7 
                   −13.623 
                   34.973 
                   15.243 
                 
                   ATOM 
                   556 
                   CA 
                   CYS 
                   A 
                   7 
                   −13.931 
                   34.328 
                   13.969 
                 
                   ATOM 
                   557 
                   C 
                   CYS 
                   A 
                   7 
                   −13.091 
                   33.071 
                   13.798 
                 
                   ATOM 
                   558 
                   O 
                   CYS 
                   A 
                   7 
                   −11.961 
                   33.123 
                   13.302 
                 
                   ATOM 
                   559 
                   CB 
                   CYS 
                   A 
                   7 
                   −13.653 
                   35.290 
                   12.824 
                 
                   ATOM 
                   560 
                   SG 
                   CYS 
                   A 
                   7 
                   −13.930 
                   34.633 
                   11.154 
                 
                   ATOM 
                   561 
                   N 
                   VAL 
                   A 
                   8 
                   −13.654 
                   31.941 
                   14.209 
                 
                   ATOM 
                   562 
                   CA 
                   VAL 
                   A 
                   8 
                   −12.949 
                   30.684 
                   14.110 
                 
                   ATOM 
                   563 
                   C 
                   VAL 
                   A 
                   8 
                   −13.653 
                   29.733 
                   13.157 
                 
                   ATOM 
                   564 
                   O 
                   VAL 
                   A 
                   8 
                   −14.759 
                   30.016 
                   12.687 
                 
                   ATOM 
                   565 
                   CB 
                   VAL 
                   A 
                   8 
                   −12.814 
                   30.038 
                   15.492 
                 
                   ATOM 
                   566 
                   CG1 
                   VAL 
                   A 
                   8 
                   −11.807 
                   30.825 
                   16.337 
                 
                   ATOM 
                   567 
                   CG2 
                   VAL 
                   A 
                   8 
                   −14.161 
                   30.006 
                   16.170 
                 
                   ATOM 
                   568 
                   N 
                   PRO 
                   A 
                   9 
                   −13.003 
                   28.601 
                   12.828 
                 
                   ATOM 
                   569 
                   CA 
                   PRO 
                   A 
                   9 
                   −13.593 
                   27.615 
                   11.918 
                 
                   ATOM 
                   570 
                   C 
                   PRO 
                   A 
                   9 
                   −14.726 
                   26.886 
                   12.631 
                 
                   ATOM 
                   571 
                   O 
                   PRO 
                   A 
                   9 
                   −14.581 
                   26.476 
                   13.780 
                 
                   ATOM 
                   572 
                   CB 
                   PRO 
                   A 
                   9 
                   −12.423 
                   26.676 
                   11.601 
                 
                   ATOM 
                   573 
                   CG 
                   PRO 
                   A 
                   9 
                   −11.204 
                   27.487 
                   11.925 
                 
                   ATOM 
                   574 
                   CD 
                   PRO 
                   A 
                   9 
                   −11.620 
                   28.226 
                   13.163 
                 
                   ATOM 
                   575 
                   N 
                   THR 
                   A 
                   10 
                   −15.847 
                   26.721 
                   11.942 
                 
                   ATOM 
                   576 
                   CA 
                   THR 
                   A 
                   10 
                   −16.999 
                   26.060 
                   12.527 
                 
                   ATOM 
                   577 
                   C 
                   THR 
                   A 
                   10 
                   −17.334 
                   24.767 
                   11.804 
                 
                   ATOM 
                   578 
                   O 
                   THR 
                   A 
                   10 
                   −18.097 
                   23.943 
                   12.303 
                 
                   ATOM 
                   579 
                   CB 
                   THR 
                   A 
                   10 
                   −18.211 
                   27.010 
                   12.523 
                 
                   ATOM 
                   580 
                   OG1 
                   THR 
                   A 
                   10 
                   −18.491 
                   27.445 
                   11.185 
                 
                   ATOM 
                   581 
                   CG2 
                   THR 
                   A 
                   10 
                   −17.902 
                   28.230 
                   13.375 
                 
                   ATOM 
                   582 
                   N 
                   GLU 
                   A 
                   11 
                   −16.750 
                   24.586 
                   10.627 
                 
                   ATOM 
                   583 
                   CA 
                   GLU 
                   A 
                   11 
                   −16.980 
                   23.377 
                   9.848 
                 
                   ATOM 
                   584 
                   C 
                   GLU 
                   A 
                   11 
                   −15.643 
                   22.935 
                   9.246 
                 
                   ATOM 
                   585 
                   O 
                   GLU 
                   A 
                   11 
                   −15.029 
                   23.666 
                   8.464 
                 
                   ATOM 
                   586 
                   CB 
                   GLU 
                   A 
                   11 
                   −17.981 
                   23.624 
                   8.715 
                 
                   ATOM 
                   587 
                   CG 
                   GLU 
                   A 
                   11 
                   −19.421 
                   23.807 
                   9.163 
                 
                   ATOM 
                   588 
                   CD 
                   GLU 
                   A 
                   11 
                   −19.686 
                   25.166 
                   9.770 
                 
                   ATOM 
                   589 
                   OE1 
                   GLU 
                   A 
                   11 
                   −19.478 
                   26.175 
                   9.073 
                 
                   ATOM 
                   590 
                   OE2 
                   GLU 
                   A 
                   11 
                   −20.111 
                   25.227 
                   10.939 
                 
                   ATOM 
                   591 
                   N 
                   LEU 
                   A 
                   12 
                   −15.183 
                   21.749 
                   9.622 
                 
                   ATOM 
                   592 
                   CA 
                   LEU 
                   A 
                   12 
                   −13.923 
                   21.254 
                   9.104 
                 
                   ATOM 
                   593 
                   C 
                   LEU 
                   A 
                   12 
                   −14.062 
                   19.912 
                   8.386 
                 
                   ATOM 
                   594 
                   O 
                   LEU 
                   A 
                   12 
                   −15.136 
                   19.299 
                   8.359 
                 
                   ATOM 
                   595 
                   CB 
                   LEU 
                   A 
                   12 
                   −12.893 
                   21.144 
                   10.230 
                 
                   ATOM 
                   596 
                   CG 
                   LEU 
                   A 
                   12 
                   −12.660 
                   22.422 
                   11.054 
                 
                   ATOM 
                   597 
                   CD1 
                   LEU 
                   A 
                   12 
                   −13.475 
                   22.350 
                   12.337 
                 
                   ATOM 
                   598 
                   CD2 
                   LEU 
                   A 
                   12 
                   −11.181 
                   22.586 
                   11.399 
                 
                   ATOM 
                   599 
                   N 
                   SER 
                   A 
                   13 
                   −12.971 
                   19.476 
                   7.771 
                 
                   ATOM 
                   600 
                   CA 
                   SER 
                   A 
                   13 
                   −12.964 
                   18.218 
                   7.046 
                 
                   ATOM 
                   601 
                   C 
                   SER 
                   A 
                   13 
                   −11.568 
                   17.628 
                   7.164 
                 
                   ATOM 
                   602 
                   O 
                   SER 
                   A 
                   13 
                   −10.613 
                   18.320 
                   7.550 
                 
                   ATOM 
                   603 
                   CB 
                   SER 
                   A 
                   13 
                   −13.346 
                   18.435 
                   5.578 
                 
                   ATOM 
                   604 
                   OG 
                   SER 
                   A 
                   13 
                   −12.404 
                   19.261 
                   4.923 
                 
                   ATOM 
                   605 
                   N 
                   ALA 
                   A 
                   13 
                   −11.449 
                   16.352 
                   6.818 
                 
                   ATOM 
                   606 
                   CA 
                   ALA 
                   A 
                   13 
                   −10.179 
                   15.665 
                   6.949 
                 
                   ATOM 
                   607 
                   C 
                   ALA 
                   A 
                   13 
                   −9.421 
                   15.471 
                   5.652 
                 
                   ATOM 
                   608 
                   O 
                   ALA 
                   A 
                   13 
                   −9.941 
                   15.720 
                   4.563 
                 
                   ATOM 
                   609 
                   CB 
                   ALA 
                   A 
                   13 
                   −10.413 
                   14.306 
                   7.626 
                 
                   ATOM 
                   610 
                   N 
                   ILE 
                   A 
                   14 
                   −8.171 
                   15.046 
                   5.783 
                 
                   ATOM 
                   611 
                   CA 
                   ILE 
                   A 
                   14 
                   −7.343 
                   14.746 
                   4.623 
                 
                   ATOM 
                   612 
                   C 
                   ILE 
                   A 
                   14 
                   −6.475 
                   13.559 
                   5.004 
                 
                   ATOM 
                   613 
                   O 
                   ILE 
                   A 
                   14 
                   −6.212 
                   13.316 
                   6.183 
                 
                   ATOM 
                   614 
                   CB 
                   ILE 
                   A 
                   14 
                   −6.401 
                   15.916 
                   4.183 
                 
                   ATOM 
                   615 
                   CG1 
                   ILE 
                   A 
                   14 
                   −5.284 
                   16.106 
                   5.200 
                 
                   ATOM 
                   616 
                   CG2 
                   ILE 
                   A 
                   14 
                   −7.188 
                   17.211 
                   3.982 
                 
                   ATOM 
                   617 
                   CD1 
                   ILE 
                   A 
                   14 
                   −4.173 
                   16.973 
                   4.696 
                 
                   ATOM 
                   618 
                   N 
                   SER 
                   A 
                   15 
                   −6.045 
                   12.806 
                   3.999 
                 
                   ATOM 
                   619 
                   CA 
                   SER 
                   A 
                   15 
                   −5.187 
                   11.662 
                   4.242 
                 
                   ATOM 
                   620 
                   C 
                   SER 
                   A 
                   15 
                   −3.740 
                   12.089 
                   4.217 
                 
                   ATOM 
                   621 
                   O 
                   SER 
                   A 
                   15 
                   −3.360 
                   13.020 
                   3.508 
                 
                   ATOM 
                   622 
                   CB 
                   SER 
                   A 
                   15 
                   −5.416 
                   10.584 
                   3.185 
                 
                   ATOM 
                   623 
                   OG 
                   SER 
                   A 
                   15 
                   −6.667 
                   9.971 
                   3.401 
                 
                   ATOM 
                   624 
                   N 
                   MET 
                   A 
                   16 
                   −2.933 
                   11.409 
                   5.012 
                 
                   ATOM 
                   625 
                   CA 
                   MET 
                   A 
                   16 
                   −1.518 
                   11.700 
                   5.047 
                 
                   ATOM 
                   626 
                   C 
                   MET 
                   A 
                   16 
                   −0.778 
                   10.414 
                   5.244 
                 
                   ATOM 
                   627 
                   O 
                   MET 
                   A 
                   16 
                   −1.137 
                   9.594 
                   6.078 
                 
                   ATOM 
                   628 
                   CB 
                   MET 
                   A 
                   16 
                   −1.170 
                   12.694 
                   6.164 
                 
                   ATOM 
                   629 
                   CG 
                   MET 
                   A 
                   16 
                   −1.848 
                   14.042 
                   5.974 
                 
                   ATOM 
                   630 
                   SD 
                   MET 
                   A 
                   16 
                   −1.017 
                   15.431 
                   6.760 
                 
                   ATOM 
                   631 
                   CE 
                   MET 
                   A 
                   16 
                   −0.799 
                   14.823 
                   8.475 
                 
                   ATOM 
                   632 
                   N 
                   LEU 
                   A 
                   17 
                   0.238 
                   10.231 
                   4.426 
                 
                   ATOM 
                   633 
                   CA 
                   LEU 
                   A 
                   17 
                   1.077 
                   9.065 
                   4.508 
                 
                   ATOM 
                   634 
                   C 
                   LEU 
                   A 
                   17 
                   2.289 
                   9.610 
                   5.264 
                 
                   ATOM 
                   635 
                   O 
                   LEU 
                   A 
                   17 
                   2.939 
                   10.565 
                   4.818 
                 
                   ATOM 
                   636 
                   CB 
                   LEU 
                   A 
                   17 
                   1.461 
                   8.608 
                   3.100 
                 
                   ATOM 
                   637 
                   CG 
                   LEU 
                   A 
                   17 
                   2.324 
                   7.355 
                   2.955 
                 
                   ATOM 
                   638 
                   CD1 
                   LEU 
                   A 
                   17 
                   1.553 
                   6.145 
                   3.445 
                 
                   ATOM 
                   639 
                   CD2 
                   LEU 
                   A 
                   17 
                   2.723 
                   7.190 
                   1.492 
                 
                   ATOM 
                   640 
                   N 
                   TYR 
                   A 
                   18 
                   2.581 
                   9.029 
                   6.418 
                 
                   ATOM 
                   641 
                   CA 
                   TYR 
                   A 
                   18 
                   3.706 
                   9.501 
                   7.196 
                 
                   ATOM 
                   642 
                   C 
                   TYR 
                   A 
                   18 
                   4.434 
                   8.333 
                   7.835 
                 
                   ATOM 
                   643 
                   O 
                   TYR 
                   A 
                   18 
                   4.081 
                   7.186 
                   7.603 
                 
                   ATOM 
                   644 
                   CB 
                   TYR 
                   A 
                   18 
                   3.222 
                   10.458 
                   8.281 
                 
                   ATOM 
                   645 
                   CG 
                   TYR 
                   A 
                   18 
                   2.386 
                   9.782 
                   9.346 
                 
                   ATOM 
                   646 
                   CD1 
                   TYR 
                   A 
                   18 
                   1.029 
                   9.527 
                   9.147 
                 
                   ATOM 
                   647 
                   CD2 
                   TYR 
                   A 
                   18 
                   2.961 
                   9.379 
                   10.550 
                 
                   ATOM 
                   648 
                   CE1 
                   TYR 
                   A 
                   18 
                   0.273 
                   8.894 
                   10.128 
                 
                   ATOM 
                   649 
                   CE2 
                   TYR 
                   A 
                   18 
                   2.218 
                   8.745 
                   11.526 
                 
                   ATOM 
                   650 
                   CZ 
                   TYR 
                   A 
                   18 
                   0.877 
                   8.508 
                   11.317 
                 
                   ATOM 
                   651 
                   OH 
                   TYR 
                   A 
                   18 
                   0.134 
                   7.922 
                   12.318 
                 
                   ATOM 
                   652 
                   N 
                   LEU 
                   A 
                   19 
                   5.439 
                   8.651 
                   8.650 
                 
                   ATOM 
                   653 
                   CA 
                   LEU 
                   A 
                   19 
                   6.255 
                   7.661 
                   9.347 
                 
                   ATOM 
                   654 
                   C 
                   LEU 
                   A 
                   19 
                   6.210 
                   7.946 
                   10.847 
                 
                   ATOM 
                   655 
                   O 
                   LEU 
                   A 
                   19 
                   6.685 
                   8.992 
                   11.288 
                 
                   ATOM 
                   656 
                   CB 
                   LEU 
                   A 
                   19 
                   7.701 
                   7.763 
                   8.871 
                 
                   ATOM 
                   657 
                   CG 
                   LEU 
                   A 
                   19 
                   7.901 
                   7.850 
                   7.359 
                 
                   ATOM 
                   658 
                   CD1 
                   LEU 
                   A 
                   19 
                   9.300 
                   8.379 
                   7.039 
                 
                   ATOM 
                   659 
                   CD2 
                   LEU 
                   A 
                   19 
                   7.669 
                   6.482 
                   6.748 
                 
                     
                 
             
                
               
               
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
               
            
           
         
       
     
     
         102 . The peptide of  claim 101 , that comprises a peptide PEP9, wherein the pair PEP9:PEP1 is selected from the group consisting of GIPEPXXVPTKM (SEQ ID NO: 6493):SAIS (SEQ ID NO: 6360), HVTKPTXVPTKL (SEQ ID NO: 6519):SAIS (SEQ ID NO: 6360), YVPKPXXVPTKL (SEQ ID NO: 6589):SAIS (SEQ ID NO: 6360), TVPKPXXVPTQL (SEQ ID NO: 6581):SAIS (SEQ ID NO: 6360), AVPKAXXVPTKL (SEQ ID NO: 6485):SAIS (SEQ ID NO: 6360), KVGKAXXVPTKL (SEQ ID NO: 6543):SAIS (SEQ ID NO: 6360), KASKAXXVPTKL (SEQ ID NO: 6527):SAIS (SEQ ID NO: 6360), GSAGPXXVPTKM (SEQ ID NO: 6501):SAIS (SEQ ID NO: 6360), AAPASXXVPTRL (SEQ ID NO: 6461):SAIS (SEQ ID NO: 6360), STPPTXXVPTRL (SEQ ID NO: 6573):SAIS (SEQ ID NO: 6360), HVPKPXXVPTKL (SEQ ID NO: 6509):SAIS (SEQ ID NO: 6360), RVPSTXXVPTKT (SEQ ID NO: 6555):SAIS (SEQ ID NO: 6360), ASAAPXXVPTAL (SEQ ID NO: 6469):SAIS (SEQ ID NO: 6360), ASASPXXVPTDL (SEQ ID NO: 6477):SAIS (SEQ ID NO: 6360), GIPEPXXVPEKM (SEQ ID NO: 6491):SAIS (SEQ ID NO: 6360), HVTKPTXAPTKL (SEQ ID NO: 6511):SAIS (SEQ ID NO: 6360), YVPKPXXAPTKL (SEQ ID NO: 6583):SAIS (SEQ ID NO: 6360), TVPKPXXAPTQL (SEQ ID NO: 6575):SAIS (SEQ ID NO: 6360), AVPKAXXAPTKL (SEQ ID NO: 6479):SAIS (SEQ ID NO: 6360), GSAGPXXTPTKM (SEQ ID NO: 6497):SAIS (SEQ ID NO: 6360), AAPASXXVPARL (SEQ ID NO: 6458):SAIS (SEQ ID NO: 6360), HVPKPXXAPTKL (SEQ ID NO: 6503):SAIS (SEQ ID NO: 6360), RVPSTXXAPVKT (SEQ ID NO: 6550):SAIS (SEQ ID NO: 6360), ASAAPXXVPQAL (SEQ ID NO: 6468):SAIS (SEQ ID NO: 6360), ASASPXXVSQDL (SEQ ID NO: 6478):SAIS (SEQ ID NO: 6360), ASASPXXVPQDL (SEQ ID NO: 6476):SAIS (SEQ ID NO: 6360), SSVKXQPSRVHH (SEQ ID NO: 6565):SAIS (SEQ ID NO: 6360), RNVQXRPTQVQL (SEQ ID NO: 6548):SAIS (SEQ ID NO: 6360), KIPKAXXAPTEL (SEQ ID NO: 6529):NAIS (SEQ ID NO: 6357), GIPEPXXAPTKM (SEQ ID NO: 6487):NAIS (SEQ ID NO: 6357), SIPKAXXAPTEL (SEQ ID NO: 6557):NAIS (SEQ ID NO: 6357), AVPKAXXAPTKL (SEQ ID NO: 6479):NAIS (SEQ ID NO: 6357), KVGKAXXAPTKL (SEQ ID NO: 6537):NAIS (SEQ ID NO: 6357), KASKAXXAPTKL (SEQ ID NO: 6521):NAIS (SEQ ID NO: 6357), GSAGPXXAPTKM (SEQ ID NO: 6495):NAIS (SEQ ID NO: 6357), AAPASXXAPTRL (SEQ ID NO: 6455):NAIS (SEQ ID NO: 6357), STPPTXXAPTRL (SEQ ID NO: 6567):NAIS (SEQ ID NO: 6357), RVPSTXXAPTKT (SEQ ID NO: 6549):NAIS (SEQ ID NO: 6357), ASAAPXXAPTAL (SEQ ID NO: 6463):NAIS (SEQ ID NO: 6357), ASASPXXAPTDL (SEQ ID NO: 6471):NAIS (SEQ ID NO: 6357), KIPKAXXVPTEL (SEQ ID NO: 6535):NAIS (SEQ ID NO: 6357), GIPEPXXVPEKM (SEQ ID NO: 6491):NAIS (SEQ ID NO: 6357), SIPKAXXVPTEL (SEQ ID NO: 6563):NAIS (SEQ ID NO: 6357), KVGKAXXVPTKL (SEQ ID NO: 6543):NAIS (SEQ ID NO: 6357), KASKAXXVPTKL (SEQ ID NO: 6527):NAIS (SEQ ID NO: 6357), GSAGPXXTPTKM (SEQ ID NO: 6497):NAIS (SEQ ID NO: 6357), AAPASXXVPARL (SEQ ID NO: 6458):NAIS (SEQ ID NO: 6357), STPPTXXVPTRL (SEQ ID NO: 6573):NAIS (SEQ ID NO: 6357), RVPSTXXAPVKT (SEQ ID NO: 6550):NAIS (SEQ ID NO: 6357), ASAAPXXVPQAL (SEQ ID NO: 6468):NAIS (SEQ ID NO: 6357), ASASPXXVSQDL (SEQ ID NO: 6478):NAIS (SEQ ID NO: 6357), ASASPXXVPQDL (SEQ ID NO: 6476):NAIS (SEQ ID NO: 6357), NDEGLEXVPTEE (SEQ ID NO: 6545):NAIS (SEQ ID NO: 6357), NDEGLEXVPTGQ (SEQ ID NO: 6546):NAIS (SEQ ID NO: 6357), SSVKXQPSRVHH (SEQ ID NO: 6565):NAIS (SEQ ID NO: 6357), RNVQXRPTQVQL (SEQ ID NO: 6548):NAIS (SEQ ID NO: 6357), KIPKAXXVPTEL (SEQ ID NO: 6535):SPIS (SEQ ID NO: 6364), GIPEPXXVPTKM (SEQ ID NO: 6493):SPIS (SEQ ID NO: 6364), SIPKAXXVPTEL (SEQ ID NO: 6563):SPIS (SEQ ID NO: 6364), HVTKPTXVPTKL (SEQ ID NO: 6519):SPIS (SEQ ID NO: 6364), YVPKPXXVPTKL (SEQ ID NO: 6589):SPIS (SEQ ID NO: 6364), TVPKPXXVPTQL (SEQ ID NO: 6581):SPIS (SEQ ID NO: 6364), AVPKAXXVPTKL (SEQ ID NO: 6485):SPIS (SEQ ID NO: 6364), KASKAXXVPTKL (SEQ ID NO: 6527):SPIS (SEQ ID NO: 6364), GSAGPXXVPTKM (SEQ ID NO: 6501):SPIS (SEQ ID NO: 6364), AAPASXXVPTRL (SEQ ID NO: 6461):SPIS (SEQ ID NO: 6364), STPPTXXVPTRL (SEQ ID NO: 6573):SPIS (SEQ ID NO: 6364), HVPKPXXVPTKL (SEQ ID NO: 6509):SPIS (SEQ ID NO: 6364), RVPSTXXVPTKT (SEQ ID NO: 6555):SPIS (SEQ ID NO: 6364), ASAAPXXVPTAL (SEQ ID NO: 6469):SPIS (SEQ ID NO: 6364), ASASPXXVPTDL (SEQ ID NO: 6477):SPIS (SEQ ID NO: 6364), GIPEPXXVPEKM (SEQ ID NO: 6491):SPIS (SEQ ID NO: 6364), HVTKPTXAPTKL (SEQ ID NO: 6511):SPIS (SEQ ID NO: 6364), YVPKPXXAPTKL (SEQ ID NO: 6583):SPIS (SEQ ID NO: 6364), TVPKPXXAPTQL (SEQ ID NO: 6575):SPIS (SEQ ID NO: 6364), AVPKAXXAPTKL (SEQ ID NO: 6479):SPIS (SEQ ID NO: 6364), GSAGPXXTPTKM (SEQ ID NO: 6497):SPIS (SEQ ID NO: 6364), AAPASXXVPARL (SEQ ID NO: 6458):SPIS (SEQ ID NO: 6364), HVPKPXXAPTKL (SEQ ID NO: 6503):SPIS (SEQ ID NO: 6364), RVPSTXXAPVKT (SEQ ID NO: 6550):SPIS (SEQ ID NO: 6364), ASAAPXXVPQAL (SEQ ID NO: 6468):SPIS (SEQ ID NO: 6364), ASASPXXVSQDL (SEQ ID NO: 6478):SPIS (SEQ ID NO: 6364), ASASPXXVPQDL (SEQ ID NO: 6476):SPIS (SEQ ID NO: 6364), SSVKXQPSRVHH (SEQ ID NO: 6565):SPIS (SEQ ID NO: 6364), RNVQXRPTQVQL (SEQ ID NO: 6548):SPIS (SEQ ID NO: 6364), and wherein X is C or S. 
     
     
         103 . The peptide of  claim 101 , wherein PEP1 is selected from the group consisting of SAIS, NAIS and SPIS and said peptide comprises the amino acid sequence selected from the group consisting of SEQ ID NOs: 1 to 5, 8, 11, 12, 14 to 23, 25 to 35, 43, 44, 45, 46, 47, 48, 49, 85, 86, 95 to 102, 105 to 123, 155 to 181, 208 to 234, 293 to 352, 506, 507, 510, 511, 514, 515, 520, 521, 522, 523, 1071, 1074, 1076, 1077, 1144, 1145, 1147, 1154, 1155, 1158, 1159, 1162, 1163, 1181, 1182, 1183, 1185, 1186, 1188, 1189, 1190, 1191, 1194, 1196, 1199 to 1206, 1208 to 1215, 1218, 1221, 1223, 1224, 1227, 1228, 1229, 1230, 1231, 1232, 1233, 1235, 1236, 1237, 1238, 1240, 1241, 1243, 1244, 1245, 1246, 1248, 1249, 1250, 1251, 1252, 1253, 1254, 1256, 1260 to 1270, 1272, 1273, 1274, 1275, 1276, 1279, 1280, 1282, 1283, 1285 to 1303, 1306, 1307, 1309, 1310, 1311, 1312, 1314 to 1325, 1328, 1329, 1332, 1333, 1339 to 1349, 1351, 1352, 1353, 1354, 1355, 1356, 1358, 1359, 1360, 1361, 1362, 1363, 1365, 1368, 1369, 1370, 1371, 1372, 1374, 1375, 1376, 1377, 1379, 1382 to 1391, 1394 to 1407, 1409, 1411, 1412, 1415, 1417, 1418, 1419, 1421, 1423, 1424, 1426, 1427, 1428, 1429, 1430, 1431, 1432, 1434, 1436, 1439, 1440, 1443, 1445, 1446, 1448, 1449, 1450, 1451, 1452, 1453, 1454, 1455, 1456, 1457, 1459, 1461, 1465, 1467, 1468, 1470, 1472 to 1482, 1484, 1485, 1487, 1489, 1490, 1870, 1871, 1872, 1873, 1877, 1880, 1882, 1884, 1885, 1886, 1888, 1889, 1890, 1896, 1897, 1900, 1901, 1902, 1904, 1907, 1909, 1913, 1916, 1917, 1919, 1920, 1922, 1926, 1929, 1931, 1933, 1936, 1937, 1940, 1941, 1942, 1943, 1946, 1947, 1948, 1950, 1951, 1956, 1957, 1958, 1959, 1960, 1961, 1964, 1965, 1967, 1968, 1969, 1972, 1973, 1974, 1975, 1976, 1980, 1985, 1986, 1987, 1989, 1991, 1992, 1994, 1995, 2000, 2001, 2002, 2003, 2005, 2007, 2008, 2009, 2010, 2011, 2012, 2013, 2015, 2016, 2019, 2020, 2023, 2024, 2025, 2028 to 2044, 2047, 2049, 2050, 2051, 2055, 2057, 2058, 2060, 2061, 2062, 2063, 2064, 2066, 2069, 2071, 2072, 2073, 2074, 2079, 2082, 2083, 2084, 2085, 2086, 2087, 2088, 2089, 2092, 2093, 2094, 2096, 2097, 2099, 2100, 2102, 2103, 2105, 2106, 2108, 2109, 2110, 2111, 2113, 2115, 2116, 2119, 2121 to 2130, 2132, 2137, 2138, 2140, 2142, 2145, 2146, 2147, 2148, 2149, 2150, 2154, 2156, 2157, 2158, 2159, 2160, 2161, 2163, 2164, 2165, 2166, 2167, 2168, 2170, 2172, 2178, 2179, 2180, 2181, 2182, 2183, 2191, 2192, 2195, 2197, 2198, 2199, 2200, 2808, 2809, 2810, 2811, 2812, 2814, 2817, 2819, 2824, 2825, 2826, 2827, 2828, 2829, 2831, 2833, 2835, 2837, 2838, 2839, 2841, 2843, 2846, 2849, 2853, 2855, 2856, 2858, 2860, 2862, 2863, 2864, 2865, 2867, 2869, 2870, 2871, 2872, 2873, 2875, 2876, 2879, 2880, 2881, 2883 to 2891, 2895, 2896, 2897, 2899, 2900, 2901, 2904 to 2911, 2913 to 2920, 2922, 2923, 2925, 2926, 2927, 2928, 2929, 2931, 2933, 2934, 2935, 2936, 2938, 2940, 2941, 2942, 2944, 2946, 2947, 2949, 2953, 2954, 2960, 2962 to 2968, 2970, 2971, 2973, 2974, 2975, 2976, 2979, 2980, 2981, 2983, 2984, 2985, 2986, 2987, 2988, 2990 to 3002, 3004 to 3010, 3012 to 3020, 3022, 3023, 3026, 3029, 3030, 3031, 3032, 3033, 3034, 3035, 3037, 3038, 3039, 3041 to 3049, 3051, 3052, 3053, 3054, 3055, 3056, 3057, 3059 to 3071, 3073, 3074, 3075, 3077, 3079, 3080, 3081, 3083, 3085, 3087, 3089, 3090, 3092 to 3099, 3101, 3103 to 3112, 3114, 3116, 3118, 3119, 3120, 3121, 3122, 3124 to 3132, 3134, 3135, 3136, 3137, 3139 to 3151, 3153, 3154, 3155, 3156, 3158, 3159, 3160, 3162, 3164, 3363 to 3424, 3429, 3430, 3432, 3438, 3439, 3441, 3443, 3444, 3445, 3446, 3447, 3448, 3452, 3455, 3456, 3457, 3458, 3459, 3460, 3463, 3465, 3467, 3472, 3474, 3481, 3482, 3483, 3484, 3487, 3490, 3491, 3493, 3495, 3496, 3497, 3499, 3502, 3506, 3508, 3510, 3513, 3514, 3515, 3518, 3519, 3523, 3525, 3526, 3527, 3528, 3529, 3532, 3533, 3534, 3537, 3539, 3540, 3541, 3542, 3543, 3547, 3548, 3550, 3554 to 3563, 3567, 3568, 3569, 3572, 3573, 3574, 3575, 3576, 3579, 3581, 3583, 3585, 3587, 3588, 3593, 3595, 3597, 3599, 3602, 3603, 3605, 3606, 3607, 3609, 3613, 3614, 3615, 3616, 3617, 3625, 3626, 3627, 3628, 3629, 3631, 3632, 3634, 3635, 3636, 3637, 3638, 3640, 3642, 3643, 3644, 3645, 3646, 3647, 3648, 3652, 3653, 3654, 3655, 3656, 3659, 3661, 3662, 3664, 3671 to 3684, 3688, 3690, 3691, 3692, 3696, 3697, 3704, 3707, 3708, 3710, 3711, 3713, 3714, 3715, 3716, 3718, 3719, 3720, 4527 to 4607, 4721, 4723, 4725, 4732, 4736, 4738, 4739, 4740, 4742, 4746, 4751, 4753, 4756, 4757, 4759, 4765, 4771, 4774, 4781, 4785, 4789, 4791, 4799, 4806, 4808, 4810, 4814, 4816, 4822, 4823, 4824, 4825, 4827, 4828, 4829, 4830, 4832, 4834, 4836, 4840, 4842, 4843, 4847, 4850, 4856, 4858, 4860, 4864, 4880, 4881, 4882, 4886, 4887, 4888, 4891, 4893, 4894, 4895, 4899, 4900, 4902, 4909, 4910, 4911, 4915, 4916, 4919, 4920, 4921, 4924, 4925, 4929, 4931, 4933, 4935, 4937, 4941, 4943, 4944, 4945, 4948, 4949, 4950, 4955, 4956, 4957, 4959, 4960, 4961, 4963, 4964, 4966, 4967, 4970, 4971, 4972, 4973, 4974, 4977, 4978, 4986, 4990, 4993, 4994, 4995, 4999, 5002, 5005, 5006, 5009, 5010, 5015, 5016, 5017, 5019, 5023, 5024, 5026, 5031, 5033, 5034, 5035, 5038, 5042, 5044, 5047, 5049, 5050, 5056, 5058, 5059, 5062, 5065, 5067, 5069, 5070, 5073, 5078, 5082, 5085, 5088, 5092, 5099, 5101, 5105, 5108, 5109, 5112, 5114, 5118, 5122, 5123, 5127, 5128, 5129, 5131, 5132, 5133, 5134, 5137, 5140, 5142, 5147, 5150, 5153, 5154, 5157, 5158, 5160, 5164, 5165, 5167, 5169, 5170, 5171, 5175, 5182, 5185, 5187, 5189, 5191, 5192, 5193, 5197, 5198, 5199, 5201, 5202, 5205, 5207, 5210, 5211, 5212, 5214, 5218, 5220, 5222, 5223, 5225, 5229, 5231, 5233, 5237, 5241, 5242, 5244, 5247, 5250, 5254, 5255, 5257, 5258, 5260, 5261, 5262, 5263, 5265, 5270, 5280, 5288, 5290, 5291, 5293, 5294, 5295, 5299, 5304, 5305, 5306, 5307, 5308, 5310, 5314, 5316, 5318, 5325, 5329, 5337, 5339, 5340, 5343, 5344, 5346, 5353, 5358, 5360, 5361, 5362, 5366, 5369, 5370, 5372, 5374, 5375, 5376, 5379, 5380, 5381, 5384, 5385, 5386, 5393, 5397, and 5645 to 5909. 
     
     
         104 . The peptide of  claim 101 , that comprises a peptide PEP9, wherein PEP1 is SAIS and wherein the pair PEP9:PEP1 is selected from the group consisting of GIPEPXXVPTKM (SEQ ID NO: 6493):SAIS (SEQ ID NO: 6360), HVTKPTXVPTKL (SEQ ID NO: 6519):SAIS (SEQ ID NO: 6360), YVPKPXXVPTKL (SEQ ID NO: 6589):SAIS (SEQ ID NO: 6360), TVPKPXXVPTQL (SEQ ID NO: 6581):SAIS (SEQ ID NO: 6360), AVPKAXXVPTKL (SEQ ID NO: 6485):SAIS (SEQ ID NO: 6360), KVGKAXXVPTKL (SEQ ID NO: 6543):SAIS (SEQ ID NO: 6360), KASKAXXVPTKL (SEQ ID NO: 6527):SAIS (SEQ ID NO: 6360), GSAGPXXVPTKM (SEQ ID NO: 6501):SAIS (SEQ ID NO: 6360), AAPASXXVPTRL (SEQ ID NO: 6461):SAIS (SEQ ID NO: 6360), STPPTXXVPTRL (SEQ ID NO: 6573):SAIS (SEQ ID NO: 6360), HVPKPXXVPTKL (SEQ ID NO: 6509):SAIS (SEQ ID NO: 6360), RVPSTXXVPTKT (SEQ ID NO: 6555):SAIS (SEQ ID NO: 6360), ASAAPXXVPTAL (SEQ ID NO: 6469):SAIS (SEQ ID NO: 6360), ASASPXXVPTDL (SEQ ID NO: 6477):SAIS (SEQ ID NO: 6360), GIPEPXXVPEKM (SEQ ID NO: 6491):SAIS (SEQ ID NO: 6360), HVTKPTXAPTKL (SEQ ID NO: 6511):SAIS (SEQ ID NO: 6360), YVPKPXXAPTKL (SEQ ID NO: 6583):SAIS (SEQ ID NO: 6360), TVPKPXXAPTQL (SEQ ID NO: 6575):SAIS (SEQ ID NO: 6360), AVPKAXXAPTKL (SEQ ID NO: 6479):SAIS (SEQ ID NO: 6360), GSAGPXXTPTKM (SEQ ID NO: 6497):SAIS (SEQ ID NO: 6360), AAPASXXVPARL (SEQ ID NO: 6458):SAIS (SEQ ID NO: 6360), HVPKPXXAPTKL (SEQ ID NO: 6503):SAIS (SEQ ID NO: 6360), RVPSTXXAPVKT (SEQ ID NO: 6550):SAIS (SEQ ID NO: 6360), ASAAPXXVPQAL (SEQ ID NO: 6468):SAIS (SEQ ID NO: 6360), ASASPXXVSQDL (SEQ ID NO: 6478):SAIS (SEQ ID NO: 6360), ASASPXXVPQDL (SEQ ID NO: 6476):SAIS (SEQ ID NO: 6360), SSVKXQPSRVHH (SEQ ID NO: 6565):SAIS (SEQ ID NO: 6360) and RNVQXRPTQVQL (SEQ ID NO: 6548):SAIS (SEQ ID NO: 6360), 
     
     
         105 . The peptide of  claim 101 , wherein PEP1 is SAIS and said peptide comprises the amino acid sequence selected from the group consisting of SEQ ID NOs: 1, 2, 3, 12, 14, 15, 18 to 23, 26, 27, 28, 33, 34, 35, 95, 96, 102, 105 to 123, 506, 507, 1071, 1144, 1154, 1155, 1181, 1182, 1188, 1190, 1191, 1199, 1202, 1203, 1205, 1206, 1208, 1211, 1212, 1213, 1214, 1229, 1230, 1231, 1235, 1236, 1238, 1243, 1244, 1248, 1252, 1256, 1262, 1263, 1268, 1272, 1275, 1286, 1288, 1291, 1292, 1294, 1295, 1296, 1299, 1300, 1302, 1306, 1307, 1309, 1310, 1311, 1316, 1317, 1319, 1320, 1333, 1345, 1347, 1349, 1354, 1358, 1359, 1361, 1363, 1368, 1369, 1370, 1371, 1374, 1376, 1379, 1382, 1384, 1390, 1391, 1397, 1399, 1401, 1402, 1426, 1428, 1430, 1445, 1449, 1451, 1453, 1476, 1479, 1484, 1487, 1871, 1877, 1882, 1884, 1885, 1902, 1904, 1909, 1916, 1917, 1926, 1936, 1943, 1946, 1964, 1965, 1969, 1974, 1975, 1976, 1985, 1987, 1994, 2002, 2012, 2016, 2019, 2028, 2030, 2032, 2034, 2038, 2039, 2041, 2042, 2049, 2055, 2060, 2061, 2066, 2073, 2082, 2083, 2084, 2086, 2094, 2096, 2099, 2100, 2102, 2103, 2105, 2109, 2110, 2116, 2119, 2123, 2125, 2126, 2145, 2147, 2148, 2150, 2158, 2160, 2163, 2164, 2166, 2181, 2183, 2192, 2198, 5646, 5648, 5649, 5650, 5653, 5654, 5659, 5660, 5661, 5663, 5664, 5667, 5668, 5671, 5672, 5673, 5674, 5675, 5676, 5680, 5683, 5684, 5685, 5686, 5687, 5689, 5693, 5694, 5696, 5699, 5700, 5701, 5702, 5705, 5706, 5707, 5710, 5713, 5714, 5715, 5716, 5718, 5719, 5721, 5722, 5724, 5725, 5726, 5729, 5730, 5732, 5733, 5734, 5735, 5736, 5737, 5742, 5744, 5748, 5751, 5752, 5753, 5754, 5758, 5760, 5763, 5764, 5766, 5767, 5771, 5774, 5775, 5776, 5779, 5780, 5783, 5785, 5786, 5787, 5788, 5789, 5792, 5793, 5794, 5795, 5796, 5798, 5799, 5800, 5804, 5807, 5808, 5809, 5811, 5817, 5819, 5822, 5823, 5825, 5827, 5828, 5831, 5832, 5836, 5837, 5839, 5840, 5841, 5842, 5845, 5846, 5851, 5856, 5859, 5860, 5866, 5867, 5868, 5871, 5873, 5874, 5875, 5877, 5878, 5881, 5883, 5884, 5885, 5886, 5891, 5892, 5894, 5896, 5897, 5898, 5899, 5901, 5903, 5904, 5906, and 5907. 
     
     
         106 . The peptide of  claim 101 , wherein the peptide is up to 25 amino acids in length. 
     
     
         107 . A peptide that is up to 30 amino acids in length and that comprises: the amino acid sequence selected from the group consisting of SEQ ID NOs: 1 to 5, 8, 11, 12, 14 to 23, 25 to 35, 43, 44, 45, 46, 47, 48, 49, 85, 86, 95 to 102, 105 to 123, 155 to 181, 208 to 234, 293 to 352, 506, 507, 510, 511, 514, 515, 520, 521, 522, 523, 1071, 1074, 1076, 1077, 1144, 1145, 1147, 1154, 1155, 1158, 1159, 1162, 1163, 1181, 1182, 1183, 1185, 1186, 1188, 1189, 1190, 1191, 1194, 1196, 1199 to 1206, 1208 to 1215, 1218, 1221, 1223, 1224, 1227, 1228, 1229, 1230, 1231, 1232, 1233, 1235, 1236, 1237, 1238, 1240, 1241, 1243, 1244, 1245, 1246, 1248, 1249, 1250, 1251, 1252, 1253, 1254, 1256, 1260 to 1270, 1272, 1273, 1274, 1275, 1276, 1279, 1280, 1282, 1283, 1285 to 1303, 1306, 1307, 1309, 1310, 1311, 1312, 1314 to 1325, 1328, 1329, 1332, 1333, 1339 to 1349, 1351, 1352, 1353, 1354, 1355, 1356, 1358, 1359, 1360, 1361, 1362, 1363, 1365, 1368, 1369, 1370, 1371, 1372, 1374, 1375, 1376, 1377, 1379, 1382 to 1391, 1394 to 1407, 1409, 1411, 1412, 1415, 1417, 1418, 1419, 1421, 1423, 1424, 1426, 1427, 1428, 1429, 1430, 1431, 1432, 1434, 1436, 1439, 1440, 1443, 1445, 1446, 1448, 1449, 1450, 1451, 1452, 1453, 1454, 1455, 1456, 1457, 1459, 1461, 1465, 1467, 1468, 1470, 1472 to 1482, 1484, 1485, 1487, 1489, 1490, 1870, 1871, 1872, 1873, 1877, 1880, 1882, 1884, 1885, 1886, 1888, 1889, 1890, 1896, 1897, 1900, 1901, 1902, 1904, 1907, 1909, 1913, 1916, 1917, 1919, 1920, 1922, 1926, 1929, 1931, 1933, 1936, 1937, 1940, 1941, 1942, 1943, 1946, 1947, 1948, 1950, 1951, 1956, 1957, 1958, 1959, 1960, 1961, 1964, 1965, 1967, 1968, 1969, 1972, 1973, 1974, 1975, 1976, 1980, 1985, 1986, 1987, 1989, 1991, 1992, 1994, 1995, 2000, 2001, 2002, 2003, 2005, 2007, 2008, 2009, 2010, 2011, 2012, 2013, 2015, 2016, 2019, 2020, 2023, 2024, 2025, 2028 to 2044, 2047, 2049, 2050, 2051, 2055, 2057, 2058, 2060, 2061, 2062, 2063, 2064, 2066, 2069, 2071, 2072, 2073, 2074, 2079, 2082, 2083, 2084, 2085, 2086, 2087, 2088, 2089, 2092, 2093, 2094, 2096, 2097, 2099, 2100, 2102, 2103, 2105, 2106, 2108, 2109, 2110, 2111, 2113, 2115, 2116, 2119, 2121 to 2130, 2132, 2137, 2138, 2140, 2142, 2145, 2146, 2147, 2148, 2149, 2150, 2154, 2156, 2157, 2158, 2159, 2160, 2161, 2163, 2164, 2165, 2166, 2167, 2168, 2170, 2172, 2178, 2179, 2180, 2181, 2182, 2183, 2191, 2192, 2195, 2197, 2198, 2199, 2200, 2808, 2809, 2810, 2811, 2812, 2814, 2817, 2819, 2824, 2825, 2826, 2827, 2828, 2829, 2831, 2833, 2835, 2837, 2838, 2839, 2841, 2843, 2846, 2849, 2853, 2855, 2856, 2858, 2860, 2862, 2863, 2864, 2865, 2867, 2869, 2870, 2871, 2872, 2873, 2875, 2876, 2879, 2880, 2881, 2883 to 2891, 2895, 2896, 2897, 2899, 2900, 2901, 2904 to 2911, 2913 to 2920, 2922, 2923, 2925, 2926, 2927, 2928, 2929, 2931, 2933, 2934, 2935, 2936, 2938, 2940, 2941, 2942, 2944, 2946, 2947, 2949, 2953, 2954, 2960, 2962 to 2968, 2970, 2971, 2973, 2974, 2975, 2976, 2979, 2980, 2981, 2983, 2984, 2985, 2986, 2987, 2988, 2990 to 3002, 3004 to 3010, 3012 to 3020, 3022, 3023, 3026, 3029, 3030, 3031, 3032, 3033, 3034, 3035, 3037, 3038, 3039, 3041 to 3049, 3051, 3052, 3053, 3054, 3055, 3056, 3057, 3059 to 3071, 3073, 3074, 3075, 3077, 3079, 3080, 3081, 3083, 3085, 3087, 3089, 3090, 3092 to 3099, 3101, 3103 to 3112, 3114, 3116, 3118, 3119, 3120, 3121, 3122, 3124 to 3132, 3134, 3135, 3136, 3137, 3139 to 3151, 3153, 3154, 3155, 3156, 3158, 3159, 3160, 3162, 3164, 3363 to 3424, 3429, 3430, 3432, 3438, 3439, 3441, 3443, 3444, 3445, 3446, 3447, 3448, 3452, 3455, 3456, 3457, 3458, 3459, 3460, 3463, 3465, 3467, 3472, 3474, 3481, 3482, 3483, 3484, 3487, 3490, 3491, 3493, 3495, 3496, 3497, 3499, 3502, 3506, 3508, 3510, 3513, 3514, 3515, 3518, 3519, 3523, 3525, 3526, 3527, 3528, 3529, 3532, 3533, 3534, 3537, 3539, 3540, 3541, 3542, 3543, 3547, 3548, 3550, 3554 to 3563, 3567, 3568, 3569, 3572, 3573, 3574, 3575, 3576, 3579, 3581, 3583, 3585, 3587, 3588, 3593, 3595, 3597, 3599, 3602, 3603, 3605, 3606, 3607, 3609, 3613, 3614, 3615, 3616, 3617, 3625, 3626, 3627, 3628, 3629, 3631, 3632, 3634, 3635, 3636, 3637, 3638, 3640, 3642, 3643, 3644, 3645, 3646, 3647, 3648, 3652, 3653, 3654, 3655, 3656, 3659, 3661, 3662, 3664, 3671 to 3684, 3688, 3690, 3691, 3692, 3696, 3697, 3704, 3707, 3708, 3710, 3711, 3713, 3714, 3715, 3716, 3718, 3719, 3720, 4527 to 4607, 4721, 4723, 4725, 4732, 4736, 4738, 4739, 4740, 4742, 4746, 4751, 4753, 4756, 4757, 4759, 4765, 4771, 4774, 4781, 4785, 4789, 4791, 4799, 4806, 4808, 4810, 4814, 4816, 4822, 4823, 4824, 4825, 4827, 4828, 4829, 4830, 4832, 4834, 4836, 4840, 4842, 4843, 4847, 4850, 4856, 4858, 4860, 4864, 4880, 4881, 4882, 4886, 4887, 4888, 4891, 4893, 4894, 4895, 4899, 4900, 4902, 4909, 4910, 4911, 4915, 4916, 4919, 4920, 4921, 4924, 4925, 4929, 4931, 4933, 4935, 4937, 4941, 4943, 4944, 4945, 4948, 4949, 4950, 4955, 4956, 4957, 4959, 4960, 4961, 4963, 4964, 4966, 4967, 4970, 4971, 4972, 4973, 4974, 4977, 4978, 4986, 4990, 4993, 4994, 4995, 4999, 5002, 5005, 5006, 5009, 5010, 5015, 5016, 5017, 5019, 5023, 5024, 5026, 5031, 5033, 5034, 5035, 5038, 5042, 5044, 5047, 5049, 5050, 5056, 5058, 5059, 5062, 5065, 5067, 5069, 5070, 5073, 5078, 5082, 5085, 5088, 5092, 5099, 5101, 5105, 5108, 5109, 5112, 5114, 5118, 5122, 5123, 5127, 5128, 5129, 5131, 5132, 5133, 5134, 5137, 5140, 5142, 5147, 5150, 5153, 5154, 5157, 5158, 5160, 5164, 5165, 5167, 5169, 5170, 5171, 5175, 5182, 5185, 5187, 5189, 5191, 5192, 5193, 5197, 5198, 5199, 5201, 5202, 5205, 5207, 5210, 5211, 5212, 5214, 5218, 5220, 5222, 5223, 5225, 5229, 5231, 5233, 5237, 5241, 5242, 5244, 5247, 5250, 5254, 5255, 5257, 5258, 5260, 5261, 5262, 5263, 5265, 5270, 5280, 5288, 5290, 5291, 5293, 5294, 5295, 5299, 5304, 5305, 5306, 5307, 5308, 5310, 5314, 5316, 5318, 5325, 5329, 5337, 5339, 5340, 5343, 5344, 5346, 5353, 5358, 5360, 5361, 5362, 5366, 5369, 5370, 5372, 5374, 5375, 5376, 5379, 5380, 5381, 5384, 5385, 5386, 5393, 5397, and 5645 to 5909; and
 at least one biomaterial-affinity-containing group, wherein said at least one biomaterial-affinity-containing group provides said peptide, with the ability to covalently or non-covalently interact with a biomaterial.   
     
     
         108 . A functionalized biomaterial comprising at least one peptide according to  claim 101 , and a biomaterial. 
     
     
         109 . A medical composition comprising at least one peptide according to  claim 101 , and a medically acceptable carrier. 
     
     
         110 . A medical composition comprising at least one peptide according to  claim 107 , and a medically acceptable carrier. 
     
     
         111 . A medical composition comprising at least one functionalized biomaterial according to  claim 108 , and a medically acceptable carrier. 
     
     
         112 . A functionalized biomaterial according to  claim 108 , wherein said biomaterial has a stiffness of at least 0.01 kPa and not more than 5 GPa. 
     
     
         113 . A functionalized biomaterial according to  claim 108 , wherein said biomaterial is selected from the group consisting of metals and alloys, ceramics, polymeric biomaterials, and biocomposite materials. 
     
     
         114 . A functionalized biomaterial according to  claim 108 , wherein said biomaterial is selected from the group consisting of a solid ceramic component, a collagen and a biodegradable hydrogel. 
     
     
         115 . A method of inducing cell differentiation, tissue regeneration, or tissue formation comprising:
 administering an effective amount of a peptide to a mesenchymal stem cell or progenitor cell at any stage of differentiation thereof,   wherein said method is selected from the group consisting of a pharmaceutical method, a surgical method, a dermatological method, a prophylactic method, an imaging method and any combination thereof,   wherein the administration is in vitro, ex vivo or in vivo, and wherein the peptide is up to 30 amino acids in length and comprises a peptide with four amino acids, PEP1;   wherein PEP1 is selected from the group consisting of SAIS, NAIS and SPIS;   wherein the RMSD value of the structure coordinates of said peptide or peptidomimetic with respect to PEPREF is 2.45 Å (Angstroms) or less;   and wherein PEPREF is   
       
         
           
                 
                 
                 
                 
                 
                 
                 
                 
                 
               
                     
                 
                   ATOM 
                   511 
                   N 
                   LYS 
                   A 
                   1 
                   −14.570 
                   46.437 
                   27.424 
                 
                   ATOM 
                   512 
                   CA 
                   LYS 
                   A 
                   1 
                   −13.512 
                   45.748 
                   28.151 
                 
                   ATOM 
                   513 
                   C 
                   LYS 
                   A 
                   1 
                   −13.655 
                   44.259 
                   27.884 
                 
                   ATOM 
                   514 
                   O 
                   LYS 
                   A 
                   1 
                   −12.769 
                   43.463 
                   28.197 
                 
                   ATOM 
                   515 
                   CB 
                   LYS 
                   A 
                   1 
                   −13.605 
                   46.029 
                   29.652 
                 
                   ATOM 
                   516 
                   CG 
                   LYS 
                   A 
                   1 
                   −13.640 
                   47.509 
                   29.991 
                 
                   ATOM 
                   517 
                   CD 
                   LYS 
                   A 
                   1 
                   −12.615 
                   48.297 
                   29.183 
                 
                   ATOM 
                   518 
                   CE 
                   LYS 
                   A 
                   1 
                   −12.625 
                   49.768 
                   29.575 
                 
                   ATOM 
                   519 
                   NZ 
                   LYS 
                   A 
                   1 
                   −13.994 
                   50.369 
                   29.497 
                 
                   ATOM 
                   520 
                   N 
                   ILE 
                   A 
                   2 
                   −14.792 
                   43.890 
                   27.309 
                 
                   ATOM 
                   521 
                   CA 
                   ILE 
                   A 
                   2 
                   −15.051 
                   42.499 
                   26.967 
                 
                   ATOM 
                   522 
                   C 
                   ILE 
                   A 
                   2 
                   −14.911 
                   42.370 
                   25.444 
                 
                   ATOM 
                   523 
                   O 
                   ILE 
                   A 
                   2 
                   −15.531 
                   43.125 
                   24.683 
                 
                   ATOM 
                   524 
                   CB 
                   ILE 
                   A 
                   2 
                   −16.466 
                   42.065 
                   27.401 
                 
                   ATOM 
                   525 
                   CG1 
                   ILE 
                   A 
                   2 
                   −16.630 
                   42.238 
                   28.915 
                 
                   ATOM 
                   526 
                   CG2 
                   ILE 
                   A 
                   2 
                   −16.710 
                   40.629 
                   26.985 
                 
                   ATOM 
                   527 
                   CD1 
                   ILE 
                   A 
                   2 
                   −15.631 
                   41.478 
                   29.30 
                 
                   ATOM 
                   528 
                   N 
                   PRO 
                   A 
                   3 
                   −14.085 
                   41.411 
                   24.989 
                 
                   ATOM 
                   529 
                   CA 
                   PRO 
                   A 
                   3 
                   −13.789 
                   41.109 
                   23.588 
                 
                   ATOM 
                   530 
                   C 
                   PRO 
                   A 
                   3 
                   −14.998 
                   40.695 
                   22.768 
                 
                   ATOM 
                   531 
                   O 
                   PRO 
                   A 
                   3 
                   −15.969 
                   40.164 
                   23.305 
                 
                   ATOM 
                   532 
                   CB 
                   PRO 
                   A 
                   3 
                   −12.785 
                   39.968 
                   23.688 
                 
                   ATOM 
                   533 
                   CG 
                   PRO 
                   A 
                   3 
                   −12.156 
                   40.166 
                   25.007 
                 
                   ATOM 
                   534 
                   CD 
                   PRO 
                   A 
                   3 
                   −13.330 
                   40.506 
                   25.867 
                 
                   ATOM 
                   535 
                   N 
                   LYS 
                   A 
                   4 
                   −14.937 
                   40.937 
                   21.463 
                 
                   ATOM 
                   536 
                   CA 
                   LYS 
                   A 
                   4 
                   −16.023 
                   40.529 
                   20.590 
                 
                   ATOM 
                   537 
                   C 
                   LYS 
                   A 
                   4 
                   −15.886 
                   39.015 
                   20.391 
                 
                   ATOM 
                   538 
                   O 
                   LYS 
                   A 
                   4 
                   −14.903 
                   38.415 
                   20.831 
                 
                   ATOM 
                   539 
                   CB 
                   LYS 
                   A 
                   4 
                   −15.926 
                   41.244 
                   19.245 
                 
                   ATOM 
                   540 
                   CG 
                   LYS 
                   A 
                   4 
                   −15.802 
                   42.751 
                   19.355 
                 
                   ATOM 
                   541 
                   CD 
                   LYS 
                   A 
                   4 
                   −16.292 
                   43.433 
                   18.083 
                 
                   ATOM 
                   542 
                   CE 
                   LYS 
                   A 
                   4 
                   −16.162 
                   44.943 
                   18.177 
                 
                   ATOM 
                   543 
                   NZ 
                   LYS 
                   A 
                   4 
                   −16.825 
                   45.628 
                   17.019 
                 
                   ATOM 
                   544 
                   N 
                   ALA 
                   A 
                   5 
                   −16.85 
                   38.393 
                   19.759 
                 
                   ATOM 
                   545 
                   CA 
                   ALA 
                   A 
                   5 
                   −16.811 
                   36.955 
                   19.507 
                 
                   ATOM 
                   546 
                   C 
                   ALA 
                   A 
                   5 
                   −15.772 
                   36.771 
                   18.416 
                 
                   ATOM 
                   547 
                   O 
                   ALA 
                   A 
                   5 
                   −15.727 
                   37.534 
                   17.455 
                 
                   ATOM 
                   548 
                   CB 
                   ALA 
                   A 
                   5 
                   −18.168 
                   36.419 
                   19.043 
                 
                   ATOM 
                   549 
                   N 
                   CYS 
                   A 
                   6 
                   −14.935 
                   35.756 
                   18.562 
                 
                   ATOM 
                   550 
                   CA 
                   CYS 
                   A 
                   6 
                   −13.887 
                   35.518 
                   17.584 
                 
                   ATOM 
                   551 
                   C 
                   CYS 
                   A 
                   6 
                   −14.347 
                   34.765 
                   16.338 
                 
                   ATOM 
                   552 
                   O 
                   CYS 
                   A 
                   6 
                   −15.327 
                   34.018 
                   16.368 
                 
                   ATOM 
                   553 
                   CB 
                   CYS 
                   A 
                   6 
                   −12.743 
                   34.768 
                   18.241 
                 
                   ATOM 
                   554 
                   SG 
                   CYS 
                   A 
                   6 
                   −11.198 
                   34.959 
                   17.353 
                 
                   ATOM 
                   555 
                   N 
                   CYS 
                   A 
                   7 
                   −13.623 
                   34.973 
                   15.243 
                 
                   ATOM 
                   556 
                   CA 
                   CYS 
                   A 
                   7 
                   −13.931 
                   34.328 
                   13.969 
                 
                   ATOM 
                   557 
                   C 
                   CYS 
                   A 
                   7 
                   −13.091 
                   33.071 
                   13.798 
                 
                   ATOM 
                   558 
                   O 
                   CYS 
                   A 
                   7 
                   −11.961 
                   33.123 
                   13.302 
                 
                   ATOM 
                   559 
                   CB 
                   CYS 
                   A 
                   7 
                   −13.653 
                   35.290 
                   12.824 
                 
                   ATOM 
                   560 
                   SG 
                   CYS 
                   A 
                   7 
                   −13.930 
                   34.633 
                   11.154 
                 
                   ATOM 
                   561 
                   N 
                   VAL 
                   A 
                   8 
                   −13.654 
                   31.941 
                   14.209 
                 
                   ATOM 
                   562 
                   CA 
                   VAL 
                   A 
                   8 
                   −12.949 
                   30.684 
                   14.110 
                 
                   ATOM 
                   563 
                   C 
                   VAL 
                   A 
                   8 
                   −13.653 
                   29.733 
                   13.157 
                 
                   ATOM 
                   564 
                   O 
                   VAL 
                   A 
                   8 
                   −14.759 
                   30.016 
                   12.687 
                 
                   ATOM 
                   565 
                   CB 
                   VAL 
                   A 
                   8 
                   −12.814 
                   30.038 
                   15.492 
                 
                   ATOM 
                   566 
                   CG1 
                   VAL 
                   A 
                   8 
                   −11.807 
                   30.825 
                   16.337 
                 
                   ATOM 
                   567 
                   CG2 
                   VAL 
                   A 
                   8 
                   −14.161 
                   30.006 
                   16.170 
                 
                   ATOM 
                   568 
                   N 
                   PRO 
                   A 
                   9 
                   −13.003 
                   28.601 
                   12.828 
                 
                   ATOM 
                   569 
                   CA 
                   PRO 
                   A 
                   9 
                   −13.593 
                   27.615 
                   11.918 
                 
                   ATOM 
                   570 
                   C 
                   PRO 
                   A 
                   9 
                   −14.726 
                   26.886 
                   12.631 
                 
                   ATOM 
                   571 
                   O 
                   PRO 
                   A 
                   9 
                   −14.581 
                   26.476 
                   13.780 
                 
                   ATOM 
                   572 
                   CB 
                   PRO 
                   A 
                   9 
                   −12.423 
                   26.676 
                   11.601 
                 
                   ATOM 
                   573 
                   CG 
                   PRO 
                   A 
                   9 
                   −11.204 
                   27.487 
                   11.925 
                 
                   ATOM 
                   574 
                   CD 
                   PRO 
                   A 
                   9 
                   −11.620 
                   28.226 
                   13.163 
                 
                   ATOM 
                   575 
                   N 
                   THR 
                   A 
                   10 
                   −15.847 
                   26.721 
                   11.942 
                 
                   ATOM 
                   576 
                   CA 
                   THR 
                   A 
                   10 
                   −16.999 
                   26.060 
                   12.527 
                 
                   ATOM 
                   577 
                   C 
                   THR 
                   A 
                   10 
                   −17.334 
                   24.767 
                   11.804 
                 
                   ATOM 
                   578 
                   O 
                   THR 
                   A 
                   10 
                   −18.097 
                   23.943 
                   12.303 
                 
                   ATOM 
                   579 
                   CB 
                   THR 
                   A 
                   10 
                   −18.211 
                   27.010 
                   12.523 
                 
                   ATOM 
                   580 
                   OG1 
                   THR 
                   A 
                   10 
                   −18.491 
                   27.445 
                   11.185 
                 
                   ATOM 
                   581 
                   CG2 
                   THR 
                   A 
                   10 
                   −17.902 
                   28.230 
                   13.375 
                 
                   ATOM 
                   582 
                   N 
                   GLU 
                   A 
                   11 
                   −16.750 
                   24.586 
                   10.627 
                 
                   ATOM 
                   583 
                   CA 
                   GLU 
                   A 
                   11 
                   −16.980 
                   23.377 
                   9.848 
                 
                   ATOM 
                   584 
                   C 
                   GLU 
                   A 
                   11 
                   −15.643 
                   22.935 
                   9.246 
                 
                   ATOM 
                   585 
                   O 
                   GLU 
                   A 
                   11 
                   −15.029 
                   23.666 
                   8.464 
                 
                   ATOM 
                   586 
                   CB 
                   GLU 
                   A 
                   11 
                   −17.981 
                   23.624 
                   8.715 
                 
                   ATOM 
                   587 
                   CG 
                   GLU 
                   A 
                   11 
                   −19.421 
                   23.807 
                   9.163 
                 
                   ATOM 
                   588 
                   CD 
                   GLU 
                   A 
                   11 
                   −19.686 
                   25.166 
                   9.770 
                 
                   ATOM 
                   589 
                   OE1 
                   GLU 
                   A 
                   11 
                   −19.478 
                   26.175 
                   9.073 
                 
                   ATOM 
                   590 
                   OE2 
                   GLU 
                   A 
                   11 
                   −20.111 
                   25.227 
                   10.939 
                 
                   ATOM 
                   591 
                   N 
                   LEU 
                   A 
                   12 
                   −15.183 
                   21.749 
                   9.622 
                 
                   ATOM 
                   592 
                   CA 
                   LEU 
                   A 
                   12 
                   −13.923 
                   21.254 
                   9.104 
                 
                   ATOM 
                   593 
                   C 
                   LEU 
                   A 
                   12 
                   −14.062 
                   19.912 
                   8.386 
                 
                   ATOM 
                   594 
                   O 
                   LEU 
                   A 
                   12 
                   −15.136 
                   19.299 
                   8.359 
                 
                   ATOM 
                   595 
                   CB 
                   LEU 
                   A 
                   12 
                   −12.893 
                   21.144 
                   10.230 
                 
                   ATOM 
                   596 
                   CG 
                   LEU 
                   A 
                   12 
                   −12.660 
                   22.422 
                   11.054 
                 
                   ATOM 
                   597 
                   CD1 
                   LEU 
                   A 
                   12 
                   −13.475 
                   22.350 
                   12.337 
                 
                   ATOM 
                   598 
                   CD2 
                   LEU 
                   A 
                   12 
                   −11.181 
                   22.586 
                   11.399 
                 
                   ATOM 
                   599 
                   N 
                   SER 
                   A 
                   13 
                   −12.971 
                   19.476 
                   7.771 
                 
                   ATOM 
                   600 
                   CA 
                   SER 
                   A 
                   13 
                   −12.964 
                   18.218 
                   7.046 
                 
                   ATOM 
                   601 
                   C 
                   SER 
                   A 
                   13 
                   −11.568 
                   17.628 
                   7.164 
                 
                   ATOM 
                   602 
                   O 
                   SER 
                   A 
                   13 
                   −10.613 
                   18.320 
                   7.550 
                 
                   ATOM 
                   603 
                   CB 
                   SER 
                   A 
                   13 
                   −13.346 
                   18.435 
                   5.578 
                 
                   ATOM 
                   604 
                   OG 
                   SER 
                   A 
                   13 
                   −12.404 
                   19.261 
                   4.923 
                 
                   ATOM 
                   605 
                   N 
                   ALA 
                   A 
                   13 
                   −11.449 
                   16.352 
                   6.818 
                 
                   ATOM 
                   606 
                   CA 
                   ALA 
                   A 
                   13 
                   −10.179 
                   15.665 
                   6.949 
                 
                   ATOM 
                   607 
                   C 
                   ALA 
                   A 
                   13 
                   −9.421 
                   15.471 
                   5.652 
                 
                   ATOM 
                   608 
                   O 
                   ALA 
                   A 
                   13 
                   −9.941 
                   15.720 
                   4.563 
                 
                   ATOM 
                   609 
                   CB 
                   ALA 
                   A 
                   13 
                   −10.413 
                   14.306 
                   7.626 
                 
                   ATOM 
                   610 
                   N 
                   ILE 
                   A 
                   14 
                   −8.171 
                   15.046 
                   5.783 
                 
                   ATOM 
                   611 
                   CA 
                   ILE 
                   A 
                   14 
                   −7.343 
                   14.746 
                   4.623 
                 
                   ATOM 
                   612 
                   C 
                   ILE 
                   A 
                   14 
                   −6.475 
                   13.559 
                   5.004 
                 
                   ATOM 
                   613 
                   O 
                   ILE 
                   A 
                   14 
                   −6.212 
                   13.316 
                   6.183 
                 
                   ATOM 
                   614 
                   CB 
                   ILE 
                   A 
                   14 
                   −6.401 
                   15.916 
                   4.183 
                 
                   ATOM 
                   615 
                   CG1 
                   ILE 
                   A 
                   14 
                   −5.284 
                   16.106 
                   5.200 
                 
                   ATOM 
                   616 
                   CG2 
                   ILE 
                   A 
                   14 
                   −7.188 
                   17.211 
                   3.982 
                 
                   ATOM 
                   617 
                   CD1 
                   ILE 
                   A 
                   14 
                   −4.173 
                   16.973 
                   4.696 
                 
                   ATOM 
                   618 
                   N 
                   SER 
                   A 
                   15 
                   −6.045 
                   12.806 
                   3.999 
                 
                   ATOM 
                   619 
                   CA 
                   SER 
                   A 
                   15 
                   −5.187 
                   11.662 
                   4.242 
                 
                   ATOM 
                   620 
                   C 
                   SER 
                   A 
                   15 
                   −3.740 
                   12.089 
                   4.217 
                 
                   ATOM 
                   621 
                   O 
                   SER 
                   A 
                   15 
                   −3.360 
                   13.020 
                   3.508 
                 
                   ATOM 
                   622 
                   CB 
                   SER 
                   A 
                   15 
                   −5.416 
                   10.584 
                   3.185 
                 
                   ATOM 
                   623 
                   OG 
                   SER 
                   A 
                   15 
                   −6.667 
                   9.971 
                   3.401 
                 
                   ATOM 
                   624 
                   N 
                   MET 
                   A 
                   16 
                   −2.933 
                   11.409 
                   5.012 
                 
                   ATOM 
                   625 
                   CA 
                   MET 
                   A 
                   16 
                   −1.518 
                   11.700 
                   5.047 
                 
                   ATOM 
                   626 
                   C 
                   MET 
                   A 
                   16 
                   −0.778 
                   10.414 
                   5.244 
                 
                   ATOM 
                   627 
                   O 
                   MET 
                   A 
                   16 
                   −1.137 
                   9.594 
                   6.078 
                 
                   ATOM 
                   628 
                   CB 
                   MET 
                   A 
                   16 
                   −1.170 
                   12.694 
                   6.164 
                 
                   ATOM 
                   629 
                   CG 
                   MET 
                   A 
                   16 
                   −1.848 
                   14.042 
                   5.974 
                 
                   ATOM 
                   630 
                   SD 
                   MET 
                   A 
                   16 
                   −1.017 
                   15.431 
                   6.760 
                 
                   ATOM 
                   631 
                   CE 
                   MET 
                   A 
                   16 
                   −0.799 
                   14.823 
                   8.475 
                 
                   ATOM 
                   632 
                   N 
                   LEU 
                   A 
                   17 
                   0.238 
                   10.231 
                   4.426 
                 
                   ATOM 
                   633 
                   CA 
                   LEU 
                   A 
                   17 
                   1.077 
                   9.065 
                   4.508 
                 
                   ATOM 
                   634 
                   C 
                   LEU 
                   A 
                   17 
                   2.289 
                   9.610 
                   5.264 
                 
                   ATOM 
                   635 
                   O 
                   LEU 
                   A 
                   17 
                   2.939 
                   10.565 
                   4.818 
                 
                   ATOM 
                   636 
                   CB 
                   LEU 
                   A 
                   17 
                   1.461 
                   8.608 
                   3.100 
                 
                   ATOM 
                   637 
                   CG 
                   LEU 
                   A 
                   17 
                   2.324 
                   7.355 
                   2.955 
                 
                   ATOM 
                   638 
                   CD1 
                   LEU 
                   A 
                   17 
                   1.553 
                   6.145 
                   3.445 
                 
                   ATOM 
                   639 
                   CD2 
                   LEU 
                   A 
                   17 
                   2.723 
                   7.190 
                   1.492 
                 
                   ATOM 
                   640 
                   N 
                   TYR 
                   A 
                   18 
                   2.581 
                   9.029 
                   6.418 
                 
                   ATOM 
                   641 
                   CA 
                   TYR 
                   A 
                   18 
                   3.706 
                   9.501 
                   7.196 
                 
                   ATOM 
                   642 
                   C 
                   TYR 
                   A 
                   18 
                   4.434 
                   8.333 
                   7.835 
                 
                   ATOM 
                   643 
                   O 
                   TYR 
                   A 
                   18 
                   4.081 
                   7.186 
                   7.603 
                 
                   ATOM 
                   644 
                   CB 
                   TYR 
                   A 
                   18 
                   3.222 
                   10.458 
                   8.281 
                 
                   ATOM 
                   645 
                   CG 
                   TYR 
                   A 
                   18 
                   2.386 
                   9.782 
                   9.346 
                 
                   ATOM 
                   646 
                   CD1 
                   TYR 
                   A 
                   18 
                   1.029 
                   9.527 
                   9.147 
                 
                   ATOM 
                   647 
                   CD2 
                   TYR 
                   A 
                   18 
                   2.961 
                   9.379 
                   10.550 
                 
                   ATOM 
                   648 
                   CE1 
                   TYR 
                   A 
                   18 
                   0.273 
                   8.894 
                   10.128 
                 
                   ATOM 
                   649 
                   CE2 
                   TYR 
                   A 
                   18 
                   2.218 
                   8.745 
                   11.526 
                 
                   ATOM 
                   650 
                   CZ 
                   TYR 
                   A 
                   18 
                   0.877 
                   8.508 
                   11.317 
                 
                   ATOM 
                   651 
                   OH 
                   TYR 
                   A 
                   18 
                   0.134 
                   7.922 
                   12.318 
                 
                   ATOM 
                   652 
                   N 
                   LEU 
                   A 
                   19 
                   5.439 
                   8.651 
                   8.650 
                 
                   ATOM 
                   653 
                   CA 
                   LEU 
                   A 
                   19 
                   6.255 
                   7.661 
                   9.347 
                 
                   ATOM 
                   654 
                   C 
                   LEU 
                   A 
                   19 
                   6.210 
                   7.946 
                   10.847 
                 
                   ATOM 
                   655 
                   O 
                   LEU 
                   A 
                   19 
                   6.685 
                   8.992 
                   11.288 
                 
                   ATOM 
                   656 
                   CB 
                   LEU 
                   A 
                   19 
                   7.701 
                   7.763 
                   8.871 
                 
                   ATOM 
                   657 
                   CG 
                   LEU 
                   A 
                   19 
                   7.901 
                   7.850 
                   7.359 
                 
                   ATOM 
                   658 
                   CD1 
                   LEU 
                   A 
                   19 
                   9.300 
                   8.379 
                   7.039 
                 
                   ATOM 
                   659 
                   CD2 
                   LEU 
                   A 
                   19 
                   7.669 
                   6.482 
                   6.748 
                 
                     
                 
             
                
               
               
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
               
            
           
         
       
     
     
         116 . A method of inducing cell differentiation, tissue regeneration, or tissue formation comprising:
 administering an effective amount of a functionalized biomaterial to a mesenchymal stem cell or progenitor cell at any stage of differentiation thereof,   wherein said method is selected from the group consisting of a pharmaceutical method, a surgical method, a dermatological method, a prophylactic method, an imaging method and any combination thereof,   wherein the administration is in vitro, ex vivo or in vivo, and   wherein the functionalized biomaterial comprises at least one peptide and at least one biomaterial-affinity-containing group, wherein said at least one biomaterial-affinity-containing group provides said peptide with the ability to covalently or non-covalently interact with a biomaterial, and   a biomaterial, and   wherein said at least one peptide is up to 30 amino acids in length and comprises a peptide with four amino acids, PEP1;   wherein PEP1 is selected from the group consisting of SAIS, NAIS and SPIS;   wherein the RMSD value of the structure coordinates of said peptide or peptidomimetic with respect to PEPREF is 2.45 Å (Angstroms) or less;   
       and wherein PEPREF is 
       
         
           
                 
                 
                 
                 
                 
                 
                 
                 
                 
               
                     
                 
                   ATOM 
                   511 
                   N 
                   LYS 
                   A 
                   1 
                   −14.570 
                   46.437 
                   27.424 
                 
                   ATOM 
                   512 
                   CA 
                   LYS 
                   A 
                   1 
                   −13.512 
                   45.748 
                   28.151 
                 
                   ATOM 
                   513 
                   C 
                   LYS 
                   A 
                   1 
                   −13.655 
                   44.259 
                   27.884 
                 
                   ATOM 
                   514 
                   O 
                   LYS 
                   A 
                   1 
                   −12.769 
                   43.463 
                   28.197 
                 
                   ATOM 
                   515 
                   CB 
                   LYS 
                   A 
                   1 
                   −13.605 
                   46.029 
                   29.652 
                 
                   ATOM 
                   516 
                   CG 
                   LYS 
                   A 
                   1 
                   −13.640 
                   47.509 
                   29.991 
                 
                   ATOM 
                   517 
                   CD 
                   LYS 
                   A 
                   1 
                   −12.615 
                   48.297 
                   29.183 
                 
                   ATOM 
                   518 
                   CE 
                   LYS 
                   A 
                   1 
                   −12.625 
                   49.768 
                   29.575 
                 
                   ATOM 
                   519 
                   NZ 
                   LYS 
                   A 
                   1 
                   −13.994 
                   50.369 
                   29.497 
                 
                   ATOM 
                   520 
                   N 
                   ILE 
                   A 
                   2 
                   −14.792 
                   43.890 
                   27.309 
                 
                   ATOM 
                   521 
                   CA 
                   ILE 
                   A 
                   2 
                   −15.051 
                   42.499 
                   26.967 
                 
                   ATOM 
                   522 
                   C 
                   ILE 
                   A 
                   2 
                   −14.911 
                   42.370 
                   25.444 
                 
                   ATOM 
                   523 
                   O 
                   ILE 
                   A 
                   2 
                   −15.531 
                   43.125 
                   24.683 
                 
                   ATOM 
                   524 
                   CB 
                   ILE 
                   A 
                   2 
                   −16.466 
                   42.065 
                   27.401 
                 
                   ATOM 
                   525 
                   CG1 
                   ILE 
                   A 
                   2 
                   −16.630 
                   42.238 
                   28.915 
                 
                   ATOM 
                   526 
                   CG2 
                   ILE 
                   A 
                   2 
                   −16.710 
                   40.629 
                   26.985 
                 
                   ATOM 
                   527 
                   CD1 
                   ILE 
                   A 
                   2 
                   −15.631 
                   41.478 
                   29.30 
                 
                   ATOM 
                   528 
                   N 
                   PRO 
                   A 
                   3 
                   −14.085 
                   41.411 
                   24.989 
                 
                   ATOM 
                   529 
                   CA 
                   PRO 
                   A 
                   3 
                   −13.789 
                   41.109 
                   23.588 
                 
                   ATOM 
                   530 
                   C 
                   PRO 
                   A 
                   3 
                   −14.998 
                   40.695 
                   22.768 
                 
                   ATOM 
                   531 
                   O 
                   PRO 
                   A 
                   3 
                   −15.969 
                   40.164 
                   23.305 
                 
                   ATOM 
                   532 
                   CB 
                   PRO 
                   A 
                   3 
                   −12.785 
                   39.968 
                   23.688 
                 
                   ATOM 
                   533 
                   CG 
                   PRO 
                   A 
                   3 
                   −12.156 
                   40.166 
                   25.007 
                 
                   ATOM 
                   534 
                   CD 
                   PRO 
                   A 
                   3 
                   −13.330 
                   40.506 
                   25.867 
                 
                   ATOM 
                   535 
                   N 
                   LYS 
                   A 
                   4 
                   −14.937 
                   40.937 
                   21.463 
                 
                   ATOM 
                   536 
                   CA 
                   LYS 
                   A 
                   4 
                   −16.023 
                   40.529 
                   20.590 
                 
                   ATOM 
                   537 
                   C 
                   LYS 
                   A 
                   4 
                   −15.886 
                   39.015 
                   20.391 
                 
                   ATOM 
                   538 
                   O 
                   LYS 
                   A 
                   4 
                   −14.903 
                   38.415 
                   20.831 
                 
                   ATOM 
                   539 
                   CB 
                   LYS 
                   A 
                   4 
                   −15.926 
                   41.244 
                   19.245 
                 
                   ATOM 
                   540 
                   CG 
                   LYS 
                   A 
                   4 
                   −15.802 
                   42.751 
                   19.355 
                 
                   ATOM 
                   541 
                   CD 
                   LYS 
                   A 
                   4 
                   −16.292 
                   43.433 
                   18.083 
                 
                   ATOM 
                   542 
                   CE 
                   LYS 
                   A 
                   4 
                   −16.162 
                   44.943 
                   18.177 
                 
                   ATOM 
                   543 
                   NZ 
                   LYS 
                   A 
                   4 
                   −16.825 
                   45.628 
                   17.019 
                 
                   ATOM 
                   544 
                   N 
                   ALA 
                   A 
                   5 
                   −16.85 
                   38.393 
                   19.759 
                 
                   ATOM 
                   545 
                   CA 
                   ALA 
                   A 
                   5 
                   −16.811 
                   36.955 
                   19.507 
                 
                   ATOM 
                   546 
                   C 
                   ALA 
                   A 
                   5 
                   −15.772 
                   36.771 
                   18.416 
                 
                   ATOM 
                   547 
                   O 
                   ALA 
                   A 
                   5 
                   −15.727 
                   37.534 
                   17.455 
                 
                   ATOM 
                   548 
                   CB 
                   ALA 
                   A 
                   5 
                   −18.168 
                   36.419 
                   19.043 
                 
                   ATOM 
                   549 
                   N 
                   CYS 
                   A 
                   6 
                   −14.935 
                   35.756 
                   18.562 
                 
                   ATOM 
                   550 
                   CA 
                   CYS 
                   A 
                   6 
                   −13.887 
                   35.518 
                   17.584 
                 
                   ATOM 
                   551 
                   C 
                   CYS 
                   A 
                   6 
                   −14.347 
                   34.765 
                   16.338 
                 
                   ATOM 
                   552 
                   O 
                   CYS 
                   A 
                   6 
                   −15.327 
                   34.018 
                   16.368 
                 
                   ATOM 
                   553 
                   CB 
                   CYS 
                   A 
                   6 
                   −12.743 
                   34.768 
                   18.241 
                 
                   ATOM 
                   554 
                   SG 
                   CYS 
                   A 
                   6 
                   −11.198 
                   34.959 
                   17.353 
                 
                   ATOM 
                   555 
                   N 
                   CYS 
                   A 
                   7 
                   −13.623 
                   34.973 
                   15.243 
                 
                   ATOM 
                   556 
                   CA 
                   CYS 
                   A 
                   7 
                   −13.931 
                   34.328 
                   13.969 
                 
                   ATOM 
                   557 
                   C 
                   CYS 
                   A 
                   7 
                   −13.091 
                   33.071 
                   13.798 
                 
                   ATOM 
                   558 
                   O 
                   CYS 
                   A 
                   7 
                   −11.961 
                   33.123 
                   13.302 
                 
                   ATOM 
                   559 
                   CB 
                   CYS 
                   A 
                   7 
                   −13.653 
                   35.290 
                   12.824 
                 
                   ATOM 
                   560 
                   SG 
                   CYS 
                   A 
                   7 
                   −13.930 
                   34.633 
                   11.154 
                 
                   ATOM 
                   561 
                   N 
                   VAL 
                   A 
                   8 
                   −13.654 
                   31.941 
                   14.209 
                 
                   ATOM 
                   562 
                   CA 
                   VAL 
                   A 
                   8 
                   −12.949 
                   30.684 
                   14.110 
                 
                   ATOM 
                   563 
                   C 
                   VAL 
                   A 
                   8 
                   −13.653 
                   29.733 
                   13.157 
                 
                   ATOM 
                   564 
                   O 
                   VAL 
                   A 
                   8 
                   −14.759 
                   30.016 
                   12.687 
                 
                   ATOM 
                   565 
                   CB 
                   VAL 
                   A 
                   8 
                   −12.814 
                   30.038 
                   15.492 
                 
                   ATOM 
                   566 
                   CG1 
                   VAL 
                   A 
                   8 
                   −11.807 
                   30.825 
                   16.337 
                 
                   ATOM 
                   567 
                   CG2 
                   VAL 
                   A 
                   8 
                   −14.161 
                   30.006 
                   16.170 
                 
                   ATOM 
                   568 
                   N 
                   PRO 
                   A 
                   9 
                   −13.003 
                   28.601 
                   12.828 
                 
                   ATOM 
                   569 
                   CA 
                   PRO 
                   A 
                   9 
                   −13.593 
                   27.615 
                   11.918 
                 
                   ATOM 
                   570 
                   C 
                   PRO 
                   A 
                   9 
                   −14.726 
                   26.886 
                   12.631 
                 
                   ATOM 
                   571 
                   O 
                   PRO 
                   A 
                   9 
                   −14.581 
                   26.476 
                   13.780 
                 
                   ATOM 
                   572 
                   CB 
                   PRO 
                   A 
                   9 
                   −12.423 
                   26.676 
                   11.601 
                 
                   ATOM 
                   573 
                   CG 
                   PRO 
                   A 
                   9 
                   −11.204 
                   27.487 
                   11.925 
                 
                   ATOM 
                   574 
                   CD 
                   PRO 
                   A 
                   9 
                   −11.620 
                   28.226 
                   13.163 
                 
                   ATOM 
                   575 
                   N 
                   THR 
                   A 
                   10 
                   −15.847 
                   26.721 
                   11.942 
                 
                   ATOM 
                   576 
                   CA 
                   THR 
                   A 
                   10 
                   −16.999 
                   26.060 
                   12.527 
                 
                   ATOM 
                   577 
                   C 
                   THR 
                   A 
                   10 
                   −17.334 
                   24.767 
                   11.804 
                 
                   ATOM 
                   578 
                   O 
                   THR 
                   A 
                   10 
                   −18.097 
                   23.943 
                   12.303 
                 
                   ATOM 
                   579 
                   CB 
                   THR 
                   A 
                   10 
                   −18.211 
                   27.010 
                   12.523 
                 
                   ATOM 
                   580 
                   OG1 
                   THR 
                   A 
                   10 
                   −18.491 
                   27.445 
                   11.185 
                 
                   ATOM 
                   581 
                   CG2 
                   THR 
                   A 
                   10 
                   −17.902 
                   28.230 
                   13.375 
                 
                   ATOM 
                   582 
                   N 
                   GLU 
                   A 
                   11 
                   −16.750 
                   24.586 
                   10.627 
                 
                   ATOM 
                   583 
                   CA 
                   GLU 
                   A 
                   11 
                   −16.980 
                   23.377 
                   9.848 
                 
                   ATOM 
                   584 
                   C 
                   GLU 
                   A 
                   11 
                   −15.643 
                   22.935 
                   9.246 
                 
                   ATOM 
                   585 
                   O 
                   GLU 
                   A 
                   11 
                   −15.029 
                   23.666 
                   8.464 
                 
                   ATOM 
                   586 
                   CB 
                   GLU 
                   A 
                   11 
                   −17.981 
                   23.624 
                   8.715 
                 
                   ATOM 
                   587 
                   CG 
                   GLU 
                   A 
                   11 
                   −19.421 
                   23.807 
                   9.163 
                 
                   ATOM 
                   588 
                   CD 
                   GLU 
                   A 
                   11 
                   −19.686 
                   25.166 
                   9.770 
                 
                   ATOM 
                   589 
                   OE1 
                   GLU 
                   A 
                   11 
                   −19.478 
                   26.175 
                   9.073 
                 
                   ATOM 
                   590 
                   OE2 
                   GLU 
                   A 
                   11 
                   −20.111 
                   25.227 
                   10.939 
                 
                   ATOM 
                   591 
                   N 
                   LEU 
                   A 
                   12 
                   −15.183 
                   21.749 
                   9.622 
                 
                   ATOM 
                   592 
                   CA 
                   LEU 
                   A 
                   12 
                   −13.923 
                   21.254 
                   9.104 
                 
                   ATOM 
                   593 
                   C 
                   LEU 
                   A 
                   12 
                   −14.062 
                   19.912 
                   8.386 
                 
                   ATOM 
                   594 
                   O 
                   LEU 
                   A 
                   12 
                   −15.136 
                   19.299 
                   8.359 
                 
                   ATOM 
                   595 
                   CB 
                   LEU 
                   A 
                   12 
                   −12.893 
                   21.144 
                   10.230 
                 
                   ATOM 
                   596 
                   CG 
                   LEU 
                   A 
                   12 
                   −12.660 
                   22.422 
                   11.054 
                 
                   ATOM 
                   597 
                   CD1 
                   LEU 
                   A 
                   12 
                   −13.475 
                   22.350 
                   12.337 
                 
                   ATOM 
                   598 
                   CD2 
                   LEU 
                   A 
                   12 
                   −11.181 
                   22.586 
                   11.399 
                 
                   ATOM 
                   599 
                   N 
                   SER 
                   A 
                   13 
                   −12.971 
                   19.476 
                   7.771 
                 
                   ATOM 
                   600 
                   CA 
                   SER 
                   A 
                   13 
                   −12.964 
                   18.218 
                   7.046 
                 
                   ATOM 
                   601 
                   C 
                   SER 
                   A 
                   13 
                   −11.568 
                   17.628 
                   7.164 
                 
                   ATOM 
                   602 
                   O 
                   SER 
                   A 
                   13 
                   −10.613 
                   18.320 
                   7.550 
                 
                   ATOM 
                   603 
                   CB 
                   SER 
                   A 
                   13 
                   −13.346 
                   18.435 
                   5.578 
                 
                   ATOM 
                   604 
                   OG 
                   SER 
                   A 
                   13 
                   −12.404 
                   19.261 
                   4.923 
                 
                   ATOM 
                   605 
                   N 
                   ALA 
                   A 
                   13 
                   −11.449 
                   16.352 
                   6.818 
                 
                   ATOM 
                   606 
                   CA 
                   ALA 
                   A 
                   13 
                   −10.179 
                   15.665 
                   6.949 
                 
                   ATOM 
                   607 
                   C 
                   ALA 
                   A 
                   13 
                   −9.421 
                   15.471 
                   5.652 
                 
                   ATOM 
                   608 
                   O 
                   ALA 
                   A 
                   13 
                   −9.941 
                   15.720 
                   4.563 
                 
                   ATOM 
                   609 
                   CB 
                   ALA 
                   A 
                   13 
                   −10.413 
                   14.306 
                   7.626 
                 
                   ATOM 
                   610 
                   N 
                   ILE 
                   A 
                   14 
                   −8.171 
                   15.046 
                   5.783 
                 
                   ATOM 
                   611 
                   CA 
                   ILE 
                   A 
                   14 
                   −7.343 
                   14.746 
                   4.623 
                 
                   ATOM 
                   612 
                   C 
                   ILE 
                   A 
                   14 
                   −6.475 
                   13.559 
                   5.004 
                 
                   ATOM 
                   613 
                   O 
                   ILE 
                   A 
                   14 
                   −6.212 
                   13.316 
                   6.183 
                 
                   ATOM 
                   614 
                   CB 
                   ILE 
                   A 
                   14 
                   −6.401 
                   15.916 
                   4.183 
                 
                   ATOM 
                   615 
                   CG1 
                   ILE 
                   A 
                   14 
                   −5.284 
                   16.106 
                   5.200 
                 
                   ATOM 
                   616 
                   CG2 
                   ILE 
                   A 
                   14 
                   −7.188 
                   17.211 
                   3.982 
                 
                   ATOM 
                   617 
                   CD1 
                   ILE 
                   A 
                   14 
                   −4.173 
                   16.973 
                   4.696 
                 
                   ATOM 
                   618 
                   N 
                   SER 
                   A 
                   15 
                   −6.045 
                   12.806 
                   3.999 
                 
                   ATOM 
                   619 
                   CA 
                   SER 
                   A 
                   15 
                   −5.187 
                   11.662 
                   4.242 
                 
                   ATOM 
                   620 
                   C 
                   SER 
                   A 
                   15 
                   −3.740 
                   12.089 
                   4.217 
                 
                   ATOM 
                   621 
                   O 
                   SER 
                   A 
                   15 
                   −3.360 
                   13.020 
                   3.508 
                 
                   ATOM 
                   622 
                   CB 
                   SER 
                   A 
                   15 
                   −5.416 
                   10.584 
                   3.185 
                 
                   ATOM 
                   623 
                   OG 
                   SER 
                   A 
                   15 
                   −6.667 
                   9.971 
                   3.401 
                 
                   ATOM 
                   624 
                   N 
                   MET 
                   A 
                   16 
                   −2.933 
                   11.409 
                   5.012 
                 
                   ATOM 
                   625 
                   CA 
                   MET 
                   A 
                   16 
                   −1.518 
                   11.700 
                   5.047 
                 
                   ATOM 
                   626 
                   C 
                   MET 
                   A 
                   16 
                   −0.778 
                   10.414 
                   5.244 
                 
                   ATOM 
                   627 
                   O 
                   MET 
                   A 
                   16 
                   −1.137 
                   9.594 
                   6.078 
                 
                   ATOM 
                   628 
                   CB 
                   MET 
                   A 
                   16 
                   −1.170 
                   12.694 
                   6.164 
                 
                   ATOM 
                   629 
                   CG 
                   MET 
                   A 
                   16 
                   −1.848 
                   14.042 
                   5.974 
                 
                   ATOM 
                   630 
                   SD 
                   MET 
                   A 
                   16 
                   −1.017 
                   15.431 
                   6.760 
                 
                   ATOM 
                   631 
                   CE 
                   MET 
                   A 
                   16 
                   −0.799 
                   14.823 
                   8.475 
                 
                   ATOM 
                   632 
                   N 
                   LEU 
                   A 
                   17 
                   0.238 
                   10.231 
                   4.426 
                 
                   ATOM 
                   633 
                   CA 
                   LEU 
                   A 
                   17 
                   1.077 
                   9.065 
                   4.508 
                 
                   ATOM 
                   634 
                   C 
                   LEU 
                   A 
                   17 
                   2.289 
                   9.610 
                   5.264 
                 
                   ATOM 
                   635 
                   O 
                   LEU 
                   A 
                   17 
                   2.939 
                   10.565 
                   4.818 
                 
                   ATOM 
                   636 
                   CB 
                   LEU 
                   A 
                   17 
                   1.461 
                   8.608 
                   3.100 
                 
                   ATOM 
                   637 
                   CG 
                   LEU 
                   A 
                   17 
                   2.324 
                   7.355 
                   2.955 
                 
                   ATOM 
                   638 
                   CD1 
                   LEU 
                   A 
                   17 
                   1.553 
                   6.145 
                   3.445 
                 
                   ATOM 
                   639 
                   CD2 
                   LEU 
                   A 
                   17 
                   2.723 
                   7.190 
                   1.492 
                 
                   ATOM 
                   640 
                   N 
                   TYR 
                   A 
                   18 
                   2.581 
                   9.029 
                   6.418 
                 
                   ATOM 
                   641 
                   CA 
                   TYR 
                   A 
                   18 
                   3.706 
                   9.501 
                   7.196 
                 
                   ATOM 
                   642 
                   C 
                   TYR 
                   A 
                   18 
                   4.434 
                   8.333 
                   7.835 
                 
                   ATOM 
                   643 
                   O 
                   TYR 
                   A 
                   18 
                   4.081 
                   7.186 
                   7.603 
                 
                   ATOM 
                   644 
                   CB 
                   TYR 
                   A 
                   18 
                   3.222 
                   10.458 
                   8.281 
                 
                   ATOM 
                   645 
                   CG 
                   TYR 
                   A 
                   18 
                   2.386 
                   9.782 
                   9.346 
                 
                   ATOM 
                   646 
                   CD1 
                   TYR 
                   A 
                   18 
                   1.029 
                   9.527 
                   9.147 
                 
                   ATOM 
                   647 
                   CD2 
                   TYR 
                   A 
                   18 
                   2.961 
                   9.379 
                   10.550 
                 
                   ATOM 
                   648 
                   CE1 
                   TYR 
                   A 
                   18 
                   0.273 
                   8.894 
                   10.128 
                 
                   ATOM 
                   649 
                   CE2 
                   TYR 
                   A 
                   18 
                   2.218 
                   8.745 
                   11.526 
                 
                   ATOM 
                   650 
                   CZ 
                   TYR 
                   A 
                   18 
                   0.877 
                   8.508 
                   11.317 
                 
                   ATOM 
                   651 
                   OH 
                   TYR 
                   A 
                   18 
                   0.134 
                   7.922 
                   12.318 
                 
                   ATOM 
                   652 
                   N 
                   LEU 
                   A 
                   19 
                   5.439 
                   8.651 
                   8.650 
                 
                   ATOM 
                   653 
                   CA 
                   LEU 
                   A 
                   19 
                   6.255 
                   7.661 
                   9.347 
                 
                   ATOM 
                   654 
                   C 
                   LEU 
                   A 
                   19 
                   6.210 
                   7.946 
                   10.847 
                 
                   ATOM 
                   655 
                   O 
                   LEU 
                   A 
                   19 
                   6.685 
                   8.992 
                   11.288 
                 
                   ATOM 
                   656 
                   CB 
                   LEU 
                   A 
                   19 
                   7.701 
                   7.763 
                   8.871 
                 
                   ATOM 
                   657 
                   CG 
                   LEU 
                   A 
                   19 
                   7.901 
                   7.850 
                   7.359 
                 
                   ATOM 
                   658 
                   CD1 
                   LEU 
                   A 
                   19 
                   9.300 
                   8.379 
                   7.039 
                 
                   ATOM 
                   659 
                   CD2 
                   LEU 
                   A 
                   19 
                   7.669 
                   6.482 
                   6.748 
                 
                     
                 
             
                
               
               
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
               
            
           
         
       
     
     
         117 . The method according to  claim 116 , wherein said method further comprises preventing, or treating a disease, condition, disorder, or pathology, or enhancing, promoting or inducing a medical application in a patient, wherein said disease, condition, disorder, pathology or medical application is selected from the group consisting of:
 enhancing osteogenesis, inducing bone formation, inducing osteocyte maturation, or treating, or preventing osteoporosis,   enhancing chondrogenesis, inducing cartilage formation, inducing chondrocyte maturation, treating or preventing osteoarthritis, treating or preventing costochondritis, treating or preventing herniation, treating or preventing achondroplasia, treating, or preventing relapsing polychondritis;   enhancing axonal dendritic neuron growth, promoting neuron-regeneration, treating, or preventing neuron degeneration-related conditions and diseases;   enhancing fibrous tissue formation, promoting tendon and ligament regeneration, preventing, or treating tendon/ligament cell degeneration;   promoting female fertility, or treating or preventing, female infertility;   treating asthma, Chronic obstructive pulmonary disease, Chronic bronchitis, Emphysema, Cystic fibrosis, Pulmonary edema, Acute respiratory distress syndrome, Pneumoconiosis, Interstitial lung disease, Sarcoidosis, Idiopathic pulmonary fibrosis, Pulmonary embolism, Pulmonary hypertension, Pleural effusion, Pneumothorax, Mesothelioma, Granulomatosis with polyangiitis, Goodpasture syndrome, Pulmonary hyperplasia, Infant respiratory distress syndrome, Chronic obstructive pulmonary disease, Silicosis, Sleep Apnea, Severe Acute Respiratory Syndrome, Pulmonary fibrosis, Primary ciliary dyskinesia, Pneumoconiosis, Hypersensitivity Pneumonitis, Cryptogenic Organizing Pneumonia (Bronchiolitis Obliterans Organizing Pneumonia, Byssinosis, Bronchopulmonary Dysplasia, Bronchiolitis, Bronchiectasis, Asbestosis, Pertussis, Middle Eastern Respiratory Syndrome, Pneumonia, Tuberculosis, Bronchitis, Histoplasmosis, Coccidioidomycosis, and Acute bronchitis;   treating obesity, Dercum's disease, Multiple symmetric lipomatosis, Familial multiple lipomatosis, Lipodystrophy, Lipedema, and Atherosclerosis.   
     
     
         118 . A surgical method for surgical treatment comprising:
 contacting a body part of a patient to be treated with a peptide, wherein said contacting induces stem cell differentiation and tissue formation, and   wherein the peptide is up to 30 amino acids in length and comprises a peptide with four amino acids, PEP1;   wherein PEP1 is selected from the group consisting of SAIS, NAIS and SPIS;   
       wherein the RMSD value of the structure coordinates of said peptide or peptidomimetic with respect to PEPREF is 2.45 Å (Angstroms) or less;
 and wherein PEPREF is 
 
       
         
           
                 
                 
                 
                 
                 
                 
                 
                 
                 
               
                     
                 
                   ATOM 
                   511 
                   N 
                   LYS 
                   A 
                   1 
                   −14.570 
                   46.437 
                   27.424 
                 
                   ATOM 
                   512 
                   CA 
                   LYS 
                   A 
                   1 
                   −13.512 
                   45.748 
                   28.151 
                 
                   ATOM 
                   513 
                   C 
                   LYS 
                   A 
                   1 
                   −13.655 
                   44.259 
                   27.884 
                 
                   ATOM 
                   514 
                   O 
                   LYS 
                   A 
                   1 
                   −12.769 
                   43.463 
                   28.197 
                 
                   ATOM 
                   515 
                   CB 
                   LYS 
                   A 
                   1 
                   −13.605 
                   46.029 
                   29.652 
                 
                   ATOM 
                   516 
                   CG 
                   LYS 
                   A 
                   1 
                   −13.640 
                   47.509 
                   29.991 
                 
                   ATOM 
                   517 
                   CD 
                   LYS 
                   A 
                   1 
                   −12.615 
                   48.297 
                   29.183 
                 
                   ATOM 
                   518 
                   CE 
                   LYS 
                   A 
                   1 
                   −12.625 
                   49.768 
                   29.575 
                 
                   ATOM 
                   519 
                   NZ 
                   LYS 
                   A 
                   1 
                   −13.994 
                   50.369 
                   29.497 
                 
                   ATOM 
                   520 
                   N 
                   ILE 
                   A 
                   2 
                   −14.792 
                   43.890 
                   27.309 
                 
                   ATOM 
                   521 
                   CA 
                   ILE 
                   A 
                   2 
                   −15.051 
                   42.499 
                   26.967 
                 
                   ATOM 
                   522 
                   C 
                   ILE 
                   A 
                   2 
                   −14.911 
                   42.370 
                   25.444 
                 
                   ATOM 
                   523 
                   O 
                   ILE 
                   A 
                   2 
                   −15.531 
                   43.125 
                   24.683 
                 
                   ATOM 
                   524 
                   CB 
                   ILE 
                   A 
                   2 
                   −16.466 
                   42.065 
                   27.401 
                 
                   ATOM 
                   525 
                   CG1 
                   ILE 
                   A 
                   2 
                   −16.630 
                   42.238 
                   28.915 
                 
                   ATOM 
                   526 
                   CG2 
                   ILE 
                   A 
                   2 
                   −16.710 
                   40.629 
                   26.985 
                 
                   ATOM 
                   527 
                   CD1 
                   ILE 
                   A 
                   2 
                   −15.631 
                   41.478 
                   29.30 
                 
                   ATOM 
                   528 
                   N 
                   PRO 
                   A 
                   3 
                   −14.085 
                   41.411 
                   24.989 
                 
                   ATOM 
                   529 
                   CA 
                   PRO 
                   A 
                   3 
                   −13.789 
                   41.109 
                   23.588 
                 
                   ATOM 
                   530 
                   C 
                   PRO 
                   A 
                   3 
                   −14.998 
                   40.695 
                   22.768 
                 
                   ATOM 
                   531 
                   O 
                   PRO 
                   A 
                   3 
                   −15.969 
                   40.164 
                   23.305 
                 
                   ATOM 
                   532 
                   CB 
                   PRO 
                   A 
                   3 
                   −12.785 
                   39.968 
                   23.688 
                 
                   ATOM 
                   533 
                   CG 
                   PRO 
                   A 
                   3 
                   −12.156 
                   40.166 
                   25.007 
                 
                   ATOM 
                   534 
                   CD 
                   PRO 
                   A 
                   3 
                   −13.330 
                   40.506 
                   25.867 
                 
                   ATOM 
                   535 
                   N 
                   LYS 
                   A 
                   4 
                   −14.937 
                   40.937 
                   21.463 
                 
                   ATOM 
                   536 
                   CA 
                   LYS 
                   A 
                   4 
                   −16.023 
                   40.529 
                   20.590 
                 
                   ATOM 
                   537 
                   C 
                   LYS 
                   A 
                   4 
                   −15.886 
                   39.015 
                   20.391 
                 
                   ATOM 
                   538 
                   O 
                   LYS 
                   A 
                   4 
                   −14.903 
                   38.415 
                   20.831 
                 
                   ATOM 
                   539 
                   CB 
                   LYS 
                   A 
                   4 
                   −15.926 
                   41.244 
                   19.245 
                 
                   ATOM 
                   540 
                   CG 
                   LYS 
                   A 
                   4 
                   −15.802 
                   42.751 
                   19.355 
                 
                   ATOM 
                   541 
                   CD 
                   LYS 
                   A 
                   4 
                   −16.292 
                   43.433 
                   18.083 
                 
                   ATOM 
                   542 
                   CE 
                   LYS 
                   A 
                   4 
                   −16.162 
                   44.943 
                   18.177 
                 
                   ATOM 
                   543 
                   NZ 
                   LYS 
                   A 
                   4 
                   −16.825 
                   45.628 
                   17.019 
                 
                   ATOM 
                   544 
                   N 
                   ALA 
                   A 
                   5 
                   −16.85 
                   38.393 
                   19.759 
                 
                   ATOM 
                   545 
                   CA 
                   ALA 
                   A 
                   5 
                   −16.811 
                   36.955 
                   19.507 
                 
                   ATOM 
                   546 
                   C 
                   ALA 
                   A 
                   5 
                   −15.772 
                   36.771 
                   18.416 
                 
                   ATOM 
                   547 
                   O 
                   ALA 
                   A 
                   5 
                   −15.727 
                   37.534 
                   17.455 
                 
                   ATOM 
                   548 
                   CB 
                   ALA 
                   A 
                   5 
                   −18.168 
                   36.419 
                   19.043 
                 
                   ATOM 
                   549 
                   N 
                   CYS 
                   A 
                   6 
                   −14.935 
                   35.756 
                   18.562 
                 
                   ATOM 
                   550 
                   CA 
                   CYS 
                   A 
                   6 
                   −13.887 
                   35.518 
                   17.584 
                 
                   ATOM 
                   551 
                   C 
                   CYS 
                   A 
                   6 
                   −14.347 
                   34.765 
                   16.338 
                 
                   ATOM 
                   552 
                   O 
                   CYS 
                   A 
                   6 
                   −15.327 
                   34.018 
                   16.368 
                 
                   ATOM 
                   553 
                   CB 
                   CYS 
                   A 
                   6 
                   −12.743 
                   34.768 
                   18.241 
                 
                   ATOM 
                   554 
                   SG 
                   CYS 
                   A 
                   6 
                   −11.198 
                   34.959 
                   17.353 
                 
                   ATOM 
                   555 
                   N 
                   CYS 
                   A 
                   7 
                   −13.623 
                   34.973 
                   15.243 
                 
                   ATOM 
                   556 
                   CA 
                   CYS 
                   A 
                   7 
                   −13.931 
                   34.328 
                   13.969 
                 
                   ATOM 
                   557 
                   C 
                   CYS 
                   A 
                   7 
                   −13.091 
                   33.071 
                   13.798 
                 
                   ATOM 
                   558 
                   O 
                   CYS 
                   A 
                   7 
                   −11.961 
                   33.123 
                   13.302 
                 
                   ATOM 
                   559 
                   CB 
                   CYS 
                   A 
                   7 
                   −13.653 
                   35.290 
                   12.824 
                 
                   ATOM 
                   560 
                   SG 
                   CYS 
                   A 
                   7 
                   −13.930 
                   34.633 
                   11.154 
                 
                   ATOM 
                   561 
                   N 
                   VAL 
                   A 
                   8 
                   −13.654 
                   31.941 
                   14.209 
                 
                   ATOM 
                   562 
                   CA 
                   VAL 
                   A 
                   8 
                   −12.949 
                   30.684 
                   14.110 
                 
                   ATOM 
                   563 
                   C 
                   VAL 
                   A 
                   8 
                   −13.653 
                   29.733 
                   13.157 
                 
                   ATOM 
                   564 
                   O 
                   VAL 
                   A 
                   8 
                   −14.759 
                   30.016 
                   12.687 
                 
                   ATOM 
                   565 
                   CB 
                   VAL 
                   A 
                   8 
                   −12.814 
                   30.038 
                   15.492 
                 
                   ATOM 
                   566 
                   CG1 
                   VAL 
                   A 
                   8 
                   −11.807 
                   30.825 
                   16.337 
                 
                   ATOM 
                   567 
                   CG2 
                   VAL 
                   A 
                   8 
                   −14.161 
                   30.006 
                   16.170 
                 
                   ATOM 
                   568 
                   N 
                   PRO 
                   A 
                   9 
                   −13.003 
                   28.601 
                   12.828 
                 
                   ATOM 
                   569 
                   CA 
                   PRO 
                   A 
                   9 
                   −13.593 
                   27.615 
                   11.918 
                 
                   ATOM 
                   570 
                   C 
                   PRO 
                   A 
                   9 
                   −14.726 
                   26.886 
                   12.631 
                 
                   ATOM 
                   571 
                   O 
                   PRO 
                   A 
                   9 
                   −14.581 
                   26.476 
                   13.780 
                 
                   ATOM 
                   572 
                   CB 
                   PRO 
                   A 
                   9 
                   −12.423 
                   26.676 
                   11.601 
                 
                   ATOM 
                   573 
                   CG 
                   PRO 
                   A 
                   9 
                   −11.204 
                   27.487 
                   11.925 
                 
                   ATOM 
                   574 
                   CD 
                   PRO 
                   A 
                   9 
                   −11.620 
                   28.226 
                   13.163 
                 
                   ATOM 
                   575 
                   N 
                   THR 
                   A 
                   10 
                   −15.847 
                   26.721 
                   11.942 
                 
                   ATOM 
                   576 
                   CA 
                   THR 
                   A 
                   10 
                   −16.999 
                   26.060 
                   12.527 
                 
                   ATOM 
                   577 
                   C 
                   THR 
                   A 
                   10 
                   −17.334 
                   24.767 
                   11.804 
                 
                   ATOM 
                   578 
                   O 
                   THR 
                   A 
                   10 
                   −18.097 
                   23.943 
                   12.303 
                 
                   ATOM 
                   579 
                   CB 
                   THR 
                   A 
                   10 
                   −18.211 
                   27.010 
                   12.523 
                 
                   ATOM 
                   580 
                   OG1 
                   THR 
                   A 
                   10 
                   −18.491 
                   27.445 
                   11.185 
                 
                   ATOM 
                   581 
                   CG2 
                   THR 
                   A 
                   10 
                   −17.902 
                   28.230 
                   13.375 
                 
                   ATOM 
                   582 
                   N 
                   GLU 
                   A 
                   11 
                   −16.750 
                   24.586 
                   10.627 
                 
                   ATOM 
                   583 
                   CA 
                   GLU 
                   A 
                   11 
                   −16.980 
                   23.377 
                   9.848 
                 
                   ATOM 
                   584 
                   C 
                   GLU 
                   A 
                   11 
                   −15.643 
                   22.935 
                   9.246 
                 
                   ATOM 
                   585 
                   O 
                   GLU 
                   A 
                   11 
                   −15.029 
                   23.666 
                   8.464 
                 
                   ATOM 
                   586 
                   CB 
                   GLU 
                   A 
                   11 
                   −17.981 
                   23.624 
                   8.715 
                 
                   ATOM 
                   587 
                   CG 
                   GLU 
                   A 
                   11 
                   −19.421 
                   23.807 
                   9.163 
                 
                   ATOM 
                   588 
                   CD 
                   GLU 
                   A 
                   11 
                   −19.686 
                   25.166 
                   9.770 
                 
                   ATOM 
                   589 
                   OE1 
                   GLU 
                   A 
                   11 
                   −19.478 
                   26.175 
                   9.073 
                 
                   ATOM 
                   590 
                   OE2 
                   GLU 
                   A 
                   11 
                   −20.111 
                   25.227 
                   10.939 
                 
                   ATOM 
                   591 
                   N 
                   LEU 
                   A 
                   12 
                   −15.183 
                   21.749 
                   9.622 
                 
                   ATOM 
                   592 
                   CA 
                   LEU 
                   A 
                   12 
                   −13.923 
                   21.254 
                   9.104 
                 
                   ATOM 
                   593 
                   C 
                   LEU 
                   A 
                   12 
                   −14.062 
                   19.912 
                   8.386 
                 
                   ATOM 
                   594 
                   O 
                   LEU 
                   A 
                   12 
                   −15.136 
                   19.299 
                   8.359 
                 
                   ATOM 
                   595 
                   CB 
                   LEU 
                   A 
                   12 
                   −12.893 
                   21.144 
                   10.230 
                 
                   ATOM 
                   596 
                   CG 
                   LEU 
                   A 
                   12 
                   −12.660 
                   22.422 
                   11.054 
                 
                   ATOM 
                   597 
                   CD1 
                   LEU 
                   A 
                   12 
                   −13.475 
                   22.350 
                   12.337 
                 
                   ATOM 
                   598 
                   CD2 
                   LEU 
                   A 
                   12 
                   −11.181 
                   22.586 
                   11.399 
                 
                   ATOM 
                   599 
                   N 
                   SER 
                   A 
                   13 
                   −12.971 
                   19.476 
                   7.771 
                 
                   ATOM 
                   600 
                   CA 
                   SER 
                   A 
                   13 
                   −12.964 
                   18.218 
                   7.046 
                 
                   ATOM 
                   601 
                   C 
                   SER 
                   A 
                   13 
                   −11.568 
                   17.628 
                   7.164 
                 
                   ATOM 
                   602 
                   O 
                   SER 
                   A 
                   13 
                   −10.613 
                   18.320 
                   7.550 
                 
                   ATOM 
                   603 
                   CB 
                   SER 
                   A 
                   13 
                   −13.346 
                   18.435 
                   5.578 
                 
                   ATOM 
                   604 
                   OG 
                   SER 
                   A 
                   13 
                   −12.404 
                   19.261 
                   4.923 
                 
                   ATOM 
                   605 
                   N 
                   ALA 
                   A 
                   13 
                   −11.449 
                   16.352 
                   6.818 
                 
                   ATOM 
                   606 
                   CA 
                   ALA 
                   A 
                   13 
                   −10.179 
                   15.665 
                   6.949 
                 
                   ATOM 
                   607 
                   C 
                   ALA 
                   A 
                   13 
                   −9.421 
                   15.471 
                   5.652 
                 
                   ATOM 
                   608 
                   O 
                   ALA 
                   A 
                   13 
                   −9.941 
                   15.720 
                   4.563 
                 
                   ATOM 
                   609 
                   CB 
                   ALA 
                   A 
                   13 
                   −10.413 
                   14.306 
                   7.626 
                 
                   ATOM 
                   610 
                   N 
                   ILE 
                   A 
                   14 
                   −8.171 
                   15.046 
                   5.783 
                 
                   ATOM 
                   611 
                   CA 
                   ILE 
                   A 
                   14 
                   −7.343 
                   14.746 
                   4.623 
                 
                   ATOM 
                   612 
                   C 
                   ILE 
                   A 
                   14 
                   −6.475 
                   13.559 
                   5.004 
                 
                   ATOM 
                   613 
                   O 
                   ILE 
                   A 
                   14 
                   −6.212 
                   13.316 
                   6.183 
                 
                   ATOM 
                   614 
                   CB 
                   ILE 
                   A 
                   14 
                   −6.401 
                   15.916 
                   4.183 
                 
                   ATOM 
                   615 
                   CG1 
                   ILE 
                   A 
                   14 
                   −5.284 
                   16.106 
                   5.200 
                 
                   ATOM 
                   616 
                   CG2 
                   ILE 
                   A 
                   14 
                   −7.188 
                   17.211 
                   3.982 
                 
                   ATOM 
                   617 
                   CD1 
                   ILE 
                   A 
                   14 
                   −4.173 
                   16.973 
                   4.696 
                 
                   ATOM 
                   618 
                   N 
                   SER 
                   A 
                   15 
                   −6.045 
                   12.806 
                   3.999 
                 
                   ATOM 
                   619 
                   CA 
                   SER 
                   A 
                   15 
                   −5.187 
                   11.662 
                   4.242 
                 
                   ATOM 
                   620 
                   C 
                   SER 
                   A 
                   15 
                   −3.740 
                   12.089 
                   4.217 
                 
                   ATOM 
                   621 
                   O 
                   SER 
                   A 
                   15 
                   −3.360 
                   13.020 
                   3.508 
                 
                   ATOM 
                   622 
                   CB 
                   SER 
                   A 
                   15 
                   −5.416 
                   10.584 
                   3.185 
                 
                   ATOM 
                   623 
                   OG 
                   SER 
                   A 
                   15 
                   −6.667 
                   9.971 
                   3.401 
                 
                   ATOM 
                   624 
                   N 
                   MET 
                   A 
                   16 
                   −2.933 
                   11.409 
                   5.012 
                 
                   ATOM 
                   625 
                   CA 
                   MET 
                   A 
                   16 
                   −1.518 
                   11.700 
                   5.047 
                 
                   ATOM 
                   626 
                   C 
                   MET 
                   A 
                   16 
                   −0.778 
                   10.414 
                   5.244 
                 
                   ATOM 
                   627 
                   O 
                   MET 
                   A 
                   16 
                   −1.137 
                   9.594 
                   6.078 
                 
                   ATOM 
                   628 
                   CB 
                   MET 
                   A 
                   16 
                   −1.170 
                   12.694 
                   6.164 
                 
                   ATOM 
                   629 
                   CG 
                   MET 
                   A 
                   16 
                   −1.848 
                   14.042 
                   5.974 
                 
                   ATOM 
                   630 
                   SD 
                   MET 
                   A 
                   16 
                   −1.017 
                   15.431 
                   6.760 
                 
                   ATOM 
                   631 
                   CE 
                   MET 
                   A 
                   16 
                   −0.799 
                   14.823 
                   8.475 
                 
                   ATOM 
                   632 
                   N 
                   LEU 
                   A 
                   17 
                   0.238 
                   10.231 
                   4.426 
                 
                   ATOM 
                   633 
                   CA 
                   LEU 
                   A 
                   17 
                   1.077 
                   9.065 
                   4.508 
                 
                   ATOM 
                   634 
                   C 
                   LEU 
                   A 
                   17 
                   2.289 
                   9.610 
                   5.264 
                 
                   ATOM 
                   635 
                   O 
                   LEU 
                   A 
                   17 
                   2.939 
                   10.565 
                   4.818 
                 
                   ATOM 
                   636 
                   CB 
                   LEU 
                   A 
                   17 
                   1.461 
                   8.608 
                   3.100 
                 
                   ATOM 
                   637 
                   CG 
                   LEU 
                   A 
                   17 
                   2.324 
                   7.355 
                   2.955 
                 
                   ATOM 
                   638 
                   CD1 
                   LEU 
                   A 
                   17 
                   1.553 
                   6.145 
                   3.445 
                 
                   ATOM 
                   639 
                   CD2 
                   LEU 
                   A 
                   17 
                   2.723 
                   7.190 
                   1.492 
                 
                   ATOM 
                   640 
                   N 
                   TYR 
                   A 
                   18 
                   2.581 
                   9.029 
                   6.418 
                 
                   ATOM 
                   641 
                   CA 
                   TYR 
                   A 
                   18 
                   3.706 
                   9.501 
                   7.196 
                 
                   ATOM 
                   642 
                   C 
                   TYR 
                   A 
                   18 
                   4.434 
                   8.333 
                   7.835 
                 
                   ATOM 
                   643 
                   O 
                   TYR 
                   A 
                   18 
                   4.081 
                   7.186 
                   7.603 
                 
                   ATOM 
                   644 
                   CB 
                   TYR 
                   A 
                   18 
                   3.222 
                   10.458 
                   8.281 
                 
                   ATOM 
                   645 
                   CG 
                   TYR 
                   A 
                   18 
                   2.386 
                   9.782 
                   9.346 
                 
                   ATOM 
                   646 
                   CD1 
                   TYR 
                   A 
                   18 
                   1.029 
                   9.527 
                   9.147 
                 
                   ATOM 
                   647 
                   CD2 
                   TYR 
                   A 
                   18 
                   2.961 
                   9.379 
                   10.550 
                 
                   ATOM 
                   648 
                   CE1 
                   TYR 
                   A 
                   18 
                   0.273 
                   8.894 
                   10.128 
                 
                   ATOM 
                   649 
                   CE2 
                   TYR 
                   A 
                   18 
                   2.218 
                   8.745 
                   11.526 
                 
                   ATOM 
                   650 
                   CZ 
                   TYR 
                   A 
                   18 
                   0.877 
                   8.508 
                   11.317 
                 
                   ATOM 
                   651 
                   OH 
                   TYR 
                   A 
                   18 
                   0.134 
                   7.922 
                   12.318 
                 
                   ATOM 
                   652 
                   N 
                   LEU 
                   A 
                   19 
                   5.439 
                   8.651 
                   8.650 
                 
                   ATOM 
                   653 
                   CA 
                   LEU 
                   A 
                   19 
                   6.255 
                   7.661 
                   9.347 
                 
                   ATOM 
                   654 
                   C 
                   LEU 
                   A 
                   19 
                   6.210 
                   7.946 
                   10.847 
                 
                   ATOM 
                   655 
                   O 
                   LEU 
                   A 
                   19 
                   6.685 
                   8.992 
                   11.288 
                 
                   ATOM 
                   656 
                   CB 
                   LEU 
                   A 
                   19 
                   7.701 
                   7.763 
                   8.871 
                 
                   ATOM 
                   657 
                   CG 
                   LEU 
                   A 
                   19 
                   7.901 
                   7.850 
                   7.359 
                 
                   ATOM 
                   658 
                   CD1 
                   LEU 
                   A 
                   19 
                   9.300 
                   8.379 
                   7.039 
                 
                   ATOM 
                   659 
                   CD2 
                   LEU 
                   A 
                   19 
                   7.669 
                   6.482 
                   6.748 
                 
                     
                 
             
                
               
               
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
               
            
           
         
       
     
     
         119 . A surgical method for surgical treatment comprising:
 contacting a body part of a patient to be treated with a functionalized biomaterial, wherein said contacting induces stem cell differentiation and tissue formation, and wherein the functionalized biomaterial comprises at least one peptide and at least one biomaterial-affinity-containing group, wherein said at least one biomaterial-affinity-containing group provides said peptide with the ability to covalently or non-covalently interact with a biomaterial, and   a biomaterial, and   wherein said at least one peptide is up to 30 amino acids in length and comprises a peptide with four amino acids, PEP1;   wherein PEP1 is selected from the group consisting of SAIS, NAIS, and SPIS;   wherein the RMSD value of the structure coordinates of said peptide or peptidomimetic with respect to PEPREF is 2.45 Å (Angstroms) or less;   
       and wherein PEPREF is 
       
         
           
                 
                 
                 
                 
                 
                 
                 
                 
                 
               
                     
                 
                   ATOM 
                   511 
                   N 
                   LYS 
                   A 
                   1 
                   −14.570 
                   46.437 
                   27.424 
                 
                   ATOM 
                   512 
                   CA 
                   LYS 
                   A 
                   1 
                   −13.512 
                   45.748 
                   28.151 
                 
                   ATOM 
                   513 
                   C 
                   LYS 
                   A 
                   1 
                   −13.655 
                   44.259 
                   27.884 
                 
                   ATOM 
                   514 
                   O 
                   LYS 
                   A 
                   1 
                   −12.769 
                   43.463 
                   28.197 
                 
                   ATOM 
                   515 
                   CB 
                   LYS 
                   A 
                   1 
                   −13.605 
                   46.029 
                   29.652 
                 
                   ATOM 
                   516 
                   CG 
                   LYS 
                   A 
                   1 
                   −13.640 
                   47.509 
                   29.991 
                 
                   ATOM 
                   517 
                   CD 
                   LYS 
                   A 
                   1 
                   −12.615 
                   48.297 
                   29.183 
                 
                   ATOM 
                   518 
                   CE 
                   LYS 
                   A 
                   1 
                   −12.625 
                   49.768 
                   29.575 
                 
                   ATOM 
                   519 
                   NZ 
                   LYS 
                   A 
                   1 
                   −13.994 
                   50.369 
                   29.497 
                 
                   ATOM 
                   520 
                   N 
                   ILE 
                   A 
                   2 
                   −14.792 
                   43.890 
                   27.309 
                 
                   ATOM 
                   521 
                   CA 
                   ILE 
                   A 
                   2 
                   −15.051 
                   42.499 
                   26.967 
                 
                   ATOM 
                   522 
                   C 
                   ILE 
                   A 
                   2 
                   −14.911 
                   42.370 
                   25.444 
                 
                   ATOM 
                   523 
                   O 
                   ILE 
                   A 
                   2 
                   −15.531 
                   43.125 
                   24.683 
                 
                   ATOM 
                   524 
                   CB 
                   ILE 
                   A 
                   2 
                   −16.466 
                   42.065 
                   27.401 
                 
                   ATOM 
                   525 
                   CG1 
                   ILE 
                   A 
                   2 
                   −16.630 
                   42.238 
                   28.915 
                 
                   ATOM 
                   526 
                   CG2 
                   ILE 
                   A 
                   2 
                   −16.710 
                   40.629 
                   26.985 
                 
                   ATOM 
                   527 
                   CD1 
                   ILE 
                   A 
                   2 
                   −15.631 
                   41.478 
                   29.30 
                 
                   ATOM 
                   528 
                   N 
                   PRO 
                   A 
                   3 
                   −14.085 
                   41.411 
                   24.989 
                 
                   ATOM 
                   529 
                   CA 
                   PRO 
                   A 
                   3 
                   −13.789 
                   41.109 
                   23.588 
                 
                   ATOM 
                   530 
                   C 
                   PRO 
                   A 
                   3 
                   −14.998 
                   40.695 
                   22.768 
                 
                   ATOM 
                   531 
                   O 
                   PRO 
                   A 
                   3 
                   −15.969 
                   40.164 
                   23.305 
                 
                   ATOM 
                   532 
                   CB 
                   PRO 
                   A 
                   3 
                   −12.785 
                   39.968 
                   23.688 
                 
                   ATOM 
                   533 
                   CG 
                   PRO 
                   A 
                   3 
                   −12.156 
                   40.166 
                   25.007 
                 
                   ATOM 
                   534 
                   CD 
                   PRO 
                   A 
                   3 
                   −13.330 
                   40.506 
                   25.867 
                 
                   ATOM 
                   535 
                   N 
                   LYS 
                   A 
                   4 
                   −14.937 
                   40.937 
                   21.463 
                 
                   ATOM 
                   536 
                   CA 
                   LYS 
                   A 
                   4 
                   −16.023 
                   40.529 
                   20.590 
                 
                   ATOM 
                   537 
                   C 
                   LYS 
                   A 
                   4 
                   −15.886 
                   39.015 
                   20.391 
                 
                   ATOM 
                   538 
                   O 
                   LYS 
                   A 
                   4 
                   −14.903 
                   38.415 
                   20.831 
                 
                   ATOM 
                   539 
                   CB 
                   LYS 
                   A 
                   4 
                   −15.926 
                   41.244 
                   19.245 
                 
                   ATOM 
                   540 
                   CG 
                   LYS 
                   A 
                   4 
                   −15.802 
                   42.751 
                   19.355 
                 
                   ATOM 
                   541 
                   CD 
                   LYS 
                   A 
                   4 
                   −16.292 
                   43.433 
                   18.083 
                 
                   ATOM 
                   542 
                   CE 
                   LYS 
                   A 
                   4 
                   −16.162 
                   44.943 
                   18.177 
                 
                   ATOM 
                   543 
                   NZ 
                   LYS 
                   A 
                   4 
                   −16.825 
                   45.628 
                   17.019 
                 
                   ATOM 
                   544 
                   N 
                   ALA 
                   A 
                   5 
                   −16.85 
                   38.393 
                   19.759 
                 
                   ATOM 
                   545 
                   CA 
                   ALA 
                   A 
                   5 
                   −16.811 
                   36.955 
                   19.507 
                 
                   ATOM 
                   546 
                   C 
                   ALA 
                   A 
                   5 
                   −15.772 
                   36.771 
                   18.416 
                 
                   ATOM 
                   547 
                   O 
                   ALA 
                   A 
                   5 
                   −15.727 
                   37.534 
                   17.455 
                 
                   ATOM 
                   548 
                   CB 
                   ALA 
                   A 
                   5 
                   −18.168 
                   36.419 
                   19.043 
                 
                   ATOM 
                   549 
                   N 
                   CYS 
                   A 
                   6 
                   −14.935 
                   35.756 
                   18.562 
                 
                   ATOM 
                   550 
                   CA 
                   CYS 
                   A 
                   6 
                   −13.887 
                   35.518 
                   17.584 
                 
                   ATOM 
                   551 
                   C 
                   CYS 
                   A 
                   6 
                   −14.347 
                   34.765 
                   16.338 
                 
                   ATOM 
                   552 
                   O 
                   CYS 
                   A 
                   6 
                   −15.327 
                   34.018 
                   16.368 
                 
                   ATOM 
                   553 
                   CB 
                   CYS 
                   A 
                   6 
                   −12.743 
                   34.768 
                   18.241 
                 
                   ATOM 
                   554 
                   SG 
                   CYS 
                   A 
                   6 
                   −11.198 
                   34.959 
                   17.353 
                 
                   ATOM 
                   555 
                   N 
                   CYS 
                   A 
                   7 
                   −13.623 
                   34.973 
                   15.243 
                 
                   ATOM 
                   556 
                   CA 
                   CYS 
                   A 
                   7 
                   −13.931 
                   34.328 
                   13.969 
                 
                   ATOM 
                   557 
                   C 
                   CYS 
                   A 
                   7 
                   −13.091 
                   33.071 
                   13.798 
                 
                   ATOM 
                   558 
                   O 
                   CYS 
                   A 
                   7 
                   −11.961 
                   33.123 
                   13.302 
                 
                   ATOM 
                   559 
                   CB 
                   CYS 
                   A 
                   7 
                   −13.653 
                   35.290 
                   12.824 
                 
                   ATOM 
                   560 
                   SG 
                   CYS 
                   A 
                   7 
                   −13.930 
                   34.633 
                   11.154 
                 
                   ATOM 
                   561 
                   N 
                   VAL 
                   A 
                   8 
                   −13.654 
                   31.941 
                   14.209 
                 
                   ATOM 
                   562 
                   CA 
                   VAL 
                   A 
                   8 
                   −12.949 
                   30.684 
                   14.110 
                 
                   ATOM 
                   563 
                   C 
                   VAL 
                   A 
                   8 
                   −13.653 
                   29.733 
                   13.157 
                 
                   ATOM 
                   564 
                   O 
                   VAL 
                   A 
                   8 
                   −14.759 
                   30.016 
                   12.687 
                 
                   ATOM 
                   565 
                   CB 
                   VAL 
                   A 
                   8 
                   −12.814 
                   30.038 
                   15.492 
                 
                   ATOM 
                   566 
                   CG1 
                   VAL 
                   A 
                   8 
                   −11.807 
                   30.825 
                   16.337 
                 
                   ATOM 
                   567 
                   CG2 
                   VAL 
                   A 
                   8 
                   −14.161 
                   30.006 
                   16.170 
                 
                   ATOM 
                   568 
                   N 
                   PRO 
                   A 
                   9 
                   −13.003 
                   28.601 
                   12.828 
                 
                   ATOM 
                   569 
                   CA 
                   PRO 
                   A 
                   9 
                   −13.593 
                   27.615 
                   11.918 
                 
                   ATOM 
                   570 
                   C 
                   PRO 
                   A 
                   9 
                   −14.726 
                   26.886 
                   12.631 
                 
                   ATOM 
                   571 
                   O 
                   PRO 
                   A 
                   9 
                   −14.581 
                   26.476 
                   13.780 
                 
                   ATOM 
                   572 
                   CB 
                   PRO 
                   A 
                   9 
                   −12.423 
                   26.676 
                   11.601 
                 
                   ATOM 
                   573 
                   CG 
                   PRO 
                   A 
                   9 
                   −11.204 
                   27.487 
                   11.925 
                 
                   ATOM 
                   574 
                   CD 
                   PRO 
                   A 
                   9 
                   −11.620 
                   28.226 
                   13.163 
                 
                   ATOM 
                   575 
                   N 
                   THR 
                   A 
                   10 
                   −15.847 
                   26.721 
                   11.942 
                 
                   ATOM 
                   576 
                   CA 
                   THR 
                   A 
                   10 
                   −16.999 
                   26.060 
                   12.527 
                 
                   ATOM 
                   577 
                   C 
                   THR 
                   A 
                   10 
                   −17.334 
                   24.767 
                   11.804 
                 
                   ATOM 
                   578 
                   O 
                   THR 
                   A 
                   10 
                   −18.097 
                   23.943 
                   12.303 
                 
                   ATOM 
                   579 
                   CB 
                   THR 
                   A 
                   10 
                   −18.211 
                   27.010 
                   12.523 
                 
                   ATOM 
                   580 
                   OG1 
                   THR 
                   A 
                   10 
                   −18.491 
                   27.445 
                   11.185 
                 
                   ATOM 
                   581 
                   CG2 
                   THR 
                   A 
                   10 
                   −17.902 
                   28.230 
                   13.375 
                 
                   ATOM 
                   582 
                   N 
                   GLU 
                   A 
                   11 
                   −16.750 
                   24.586 
                   10.627 
                 
                   ATOM 
                   583 
                   CA 
                   GLU 
                   A 
                   11 
                   −16.980 
                   23.377 
                   9.848 
                 
                   ATOM 
                   584 
                   C 
                   GLU 
                   A 
                   11 
                   −15.643 
                   22.935 
                   9.246 
                 
                   ATOM 
                   585 
                   O 
                   GLU 
                   A 
                   11 
                   −15.029 
                   23.666 
                   8.464 
                 
                   ATOM 
                   586 
                   CB 
                   GLU 
                   A 
                   11 
                   −17.981 
                   23.624 
                   8.715 
                 
                   ATOM 
                   587 
                   CG 
                   GLU 
                   A 
                   11 
                   −19.421 
                   23.807 
                   9.163 
                 
                   ATOM 
                   588 
                   CD 
                   GLU 
                   A 
                   11 
                   −19.686 
                   25.166 
                   9.770 
                 
                   ATOM 
                   589 
                   OE1 
                   GLU 
                   A 
                   11 
                   −19.478 
                   26.175 
                   9.073 
                 
                   ATOM 
                   590 
                   OE2 
                   GLU 
                   A 
                   11 
                   −20.111 
                   25.227 
                   10.939 
                 
                   ATOM 
                   591 
                   N 
                   LEU 
                   A 
                   12 
                   −15.183 
                   21.749 
                   9.622 
                 
                   ATOM 
                   592 
                   CA 
                   LEU 
                   A 
                   12 
                   −13.923 
                   21.254 
                   9.104 
                 
                   ATOM 
                   593 
                   C 
                   LEU 
                   A 
                   12 
                   −14.062 
                   19.912 
                   8.386 
                 
                   ATOM 
                   594 
                   O 
                   LEU 
                   A 
                   12 
                   −15.136 
                   19.299 
                   8.359 
                 
                   ATOM 
                   595 
                   CB 
                   LEU 
                   A 
                   12 
                   −12.893 
                   21.144 
                   10.230 
                 
                   ATOM 
                   596 
                   CG 
                   LEU 
                   A 
                   12 
                   −12.660 
                   22.422 
                   11.054 
                 
                   ATOM 
                   597 
                   CD1 
                   LEU 
                   A 
                   12 
                   −13.475 
                   22.350 
                   12.337 
                 
                   ATOM 
                   598 
                   CD2 
                   LEU 
                   A 
                   12 
                   −11.181 
                   22.586 
                   11.399 
                 
                   ATOM 
                   599 
                   N 
                   SER 
                   A 
                   13 
                   −12.971 
                   19.476 
                   7.771 
                 
                   ATOM 
                   600 
                   CA 
                   SER 
                   A 
                   13 
                   −12.964 
                   18.218 
                   7.046 
                 
                   ATOM 
                   601 
                   C 
                   SER 
                   A 
                   13 
                   −11.568 
                   17.628 
                   7.164 
                 
                   ATOM 
                   602 
                   O 
                   SER 
                   A 
                   13 
                   −10.613 
                   18.320 
                   7.550 
                 
                   ATOM 
                   603 
                   CB 
                   SER 
                   A 
                   13 
                   −13.346 
                   18.435 
                   5.578 
                 
                   ATOM 
                   604 
                   OG 
                   SER 
                   A 
                   13 
                   −12.404 
                   19.261 
                   4.923 
                 
                   ATOM 
                   605 
                   N 
                   ALA 
                   A 
                   13 
                   −11.449 
                   16.352 
                   6.818 
                 
                   ATOM 
                   606 
                   CA 
                   ALA 
                   A 
                   13 
                   −10.179 
                   15.665 
                   6.949 
                 
                   ATOM 
                   607 
                   C 
                   ALA 
                   A 
                   13 
                   −9.421 
                   15.471 
                   5.652 
                 
                   ATOM 
                   608 
                   O 
                   ALA 
                   A 
                   13 
                   −9.941 
                   15.720 
                   4.563 
                 
                   ATOM 
                   609 
                   CB 
                   ALA 
                   A 
                   13 
                   −10.413 
                   14.306 
                   7.626 
                 
                   ATOM 
                   610 
                   N 
                   ILE 
                   A 
                   14 
                   −8.171 
                   15.046 
                   5.783 
                 
                   ATOM 
                   611 
                   CA 
                   ILE 
                   A 
                   14 
                   −7.343 
                   14.746 
                   4.623 
                 
                   ATOM 
                   612 
                   C 
                   ILE 
                   A 
                   14 
                   −6.475 
                   13.559 
                   5.004 
                 
                   ATOM 
                   613 
                   O 
                   ILE 
                   A 
                   14 
                   −6.212 
                   13.316 
                   6.183 
                 
                   ATOM 
                   614 
                   CB 
                   ILE 
                   A 
                   14 
                   −6.401 
                   15.916 
                   4.183 
                 
                   ATOM 
                   615 
                   CG1 
                   ILE 
                   A 
                   14 
                   −5.284 
                   16.106 
                   5.200 
                 
                   ATOM 
                   616 
                   CG2 
                   ILE 
                   A 
                   14 
                   −7.188 
                   17.211 
                   3.982 
                 
                   ATOM 
                   617 
                   CD1 
                   ILE 
                   A 
                   14 
                   −4.173 
                   16.973 
                   4.696 
                 
                   ATOM 
                   618 
                   N 
                   SER 
                   A 
                   15 
                   −6.045 
                   12.806 
                   3.999 
                 
                   ATOM 
                   619 
                   CA 
                   SER 
                   A 
                   15 
                   −5.187 
                   11.662 
                   4.242 
                 
                   ATOM 
                   620 
                   C 
                   SER 
                   A 
                   15 
                   −3.740 
                   12.089 
                   4.217 
                 
                   ATOM 
                   621 
                   O 
                   SER 
                   A 
                   15 
                   −3.360 
                   13.020 
                   3.508 
                 
                   ATOM 
                   622 
                   CB 
                   SER 
                   A 
                   15 
                   −5.416 
                   10.584 
                   3.185 
                 
                   ATOM 
                   623 
                   OG 
                   SER 
                   A 
                   15 
                   −6.667 
                   9.971 
                   3.401 
                 
                   ATOM 
                   624 
                   N 
                   MET 
                   A 
                   16 
                   −2.933 
                   11.409 
                   5.012 
                 
                   ATOM 
                   625 
                   CA 
                   MET 
                   A 
                   16 
                   −1.518 
                   11.700 
                   5.047 
                 
                   ATOM 
                   626 
                   C 
                   MET 
                   A 
                   16 
                   −0.778 
                   10.414 
                   5.244 
                 
                   ATOM 
                   627 
                   O 
                   MET 
                   A 
                   16 
                   −1.137 
                   9.594 
                   6.078 
                 
                   ATOM 
                   628 
                   CB 
                   MET 
                   A 
                   16 
                   −1.170 
                   12.694 
                   6.164 
                 
                   ATOM 
                   629 
                   CG 
                   MET 
                   A 
                   16 
                   −1.848 
                   14.042 
                   5.974 
                 
                   ATOM 
                   630 
                   SD 
                   MET 
                   A 
                   16 
                   −1.017 
                   15.431 
                   6.760 
                 
                   ATOM 
                   631 
                   CE 
                   MET 
                   A 
                   16 
                   −0.799 
                   14.823 
                   8.475 
                 
                   ATOM 
                   632 
                   N 
                   LEU 
                   A 
                   17 
                   0.238 
                   10.231 
                   4.426 
                 
                   ATOM 
                   633 
                   CA 
                   LEU 
                   A 
                   17 
                   1.077 
                   9.065 
                   4.508 
                 
                   ATOM 
                   634 
                   C 
                   LEU 
                   A 
                   17 
                   2.289 
                   9.610 
                   5.264 
                 
                   ATOM 
                   635 
                   O 
                   LEU 
                   A 
                   17 
                   2.939 
                   10.565 
                   4.818 
                 
                   ATOM 
                   636 
                   CB 
                   LEU 
                   A 
                   17 
                   1.461 
                   8.608 
                   3.100 
                 
                   ATOM 
                   637 
                   CG 
                   LEU 
                   A 
                   17 
                   2.324 
                   7.355 
                   2.955 
                 
                   ATOM 
                   638 
                   CD1 
                   LEU 
                   A 
                   17 
                   1.553 
                   6.145 
                   3.445 
                 
                   ATOM 
                   639 
                   CD2 
                   LEU 
                   A 
                   17 
                   2.723 
                   7.190 
                   1.492 
                 
                   ATOM 
                   640 
                   N 
                   TYR 
                   A 
                   18 
                   2.581 
                   9.029 
                   6.418 
                 
                   ATOM 
                   641 
                   CA 
                   TYR 
                   A 
                   18 
                   3.706 
                   9.501 
                   7.196 
                 
                   ATOM 
                   642 
                   C 
                   TYR 
                   A 
                   18 
                   4.434 
                   8.333 
                   7.835 
                 
                   ATOM 
                   643 
                   O 
                   TYR 
                   A 
                   18 
                   4.081 
                   7.186 
                   7.603 
                 
                   ATOM 
                   644 
                   CB 
                   TYR 
                   A 
                   18 
                   3.222 
                   10.458 
                   8.281 
                 
                   ATOM 
                   645 
                   CG 
                   TYR 
                   A 
                   18 
                   2.386 
                   9.782 
                   9.346 
                 
                   ATOM 
                   646 
                   CD1 
                   TYR 
                   A 
                   18 
                   1.029 
                   9.527 
                   9.147 
                 
                   ATOM 
                   647 
                   CD2 
                   TYR 
                   A 
                   18 
                   2.961 
                   9.379 
                   10.550 
                 
                   ATOM 
                   648 
                   CE1 
                   TYR 
                   A 
                   18 
                   0.273 
                   8.894 
                   10.128 
                 
                   ATOM 
                   649 
                   CE2 
                   TYR 
                   A 
                   18 
                   2.218 
                   8.745 
                   11.526 
                 
                   ATOM 
                   650 
                   CZ 
                   TYR 
                   A 
                   18 
                   0.877 
                   8.508 
                   11.317 
                 
                   ATOM 
                   651 
                   OH 
                   TYR 
                   A 
                   18 
                   0.134 
                   7.922 
                   12.318 
                 
                   ATOM 
                   652 
                   N 
                   LEU 
                   A 
                   19 
                   5.439 
                   8.651 
                   8.650 
                 
                   ATOM 
                   653 
                   CA 
                   LEU 
                   A 
                   19 
                   6.255 
                   7.661 
                   9.347 
                 
                   ATOM 
                   654 
                   C 
                   LEU 
                   A 
                   19 
                   6.210 
                   7.946 
                   10.847 
                 
                   ATOM 
                   655 
                   O 
                   LEU 
                   A 
                   19 
                   6.685 
                   8.992 
                   11.288 
                 
                   ATOM 
                   656 
                   CB 
                   LEU 
                   A 
                   19 
                   7.701 
                   7.763 
                   8.871 
                 
                   ATOM 
                   657 
                   CG 
                   LEU 
                   A 
                   19 
                   7.901 
                   7.850 
                   7.359 
                 
                   ATOM 
                   658 
                   CD1 
                   LEU 
                   A 
                   19 
                   9.300 
                   8.379 
                   7.039 
                 
                   ATOM 
                   659 
                   CD2 
                   LEU 
                   A 
                   19 
                   7.669 
                   6.482 
                   6.748 
                 
                     
                 
             
                
               
               
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
                
               
            
           
         
       
     
     
         120 . The functionalized biomaterial according to  claim 114 , wherein said solid ceramic component is selected from a granulated ceramic powder or ceramic scaffold; and/or a gel ceramic component. 
     
     
         121 . The functionalized biomaterial according to  claim 114 , wherein the collagen is selected from collagen type I, II, III and/or XI.

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