US2005260200A1PendingUtilityA1

Antigenic peptides reacting with anti-ovary antibodies

Assignee: BIO MERIEUXPriority: Dec 31, 1996Filed: Jun 2, 2005Published: Nov 24, 2005
Est. expiryDec 31, 2016(expired)· nominal 20-yr term from priority
C07K 14/59C07K 16/18G01N 33/689A61K 38/00G01N 2800/36
51
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Claims

Abstract

An oligopeptides comprising the following sequence Thr Gln Cys His Cys Gly Lys Cys (SEQ ID NO: 5) may be used as an antigenic compound capable of being recognized by anti-ovary antibodies and as an immunogenic compound capable of inducing the production of anti-ovary antibodies. In addition, the oligopeptides may be used to detect and/or quantify anti-ovary antibodies.

Claims

exact text as granted — not AI-modified
1 - 3 . (canceled)  
     
     
         4 . A process for detection of anti-ovary antibodies in a biological sample, comprising: 
 placing said biological sample in contact with at least one oligopeptide comprising a reference peptide sequence SEQ ID NO: 5, or any peptide sequence that is a functional variant of said reference sequence in that it displays an antigenicity and/or an immunogenicity toward anti-ovary antibodies identical or similar to the antigenicity and/or the immunogenicity of the reference peptide, and    observing the formation of an antigen-antibody complex between said oligopeptide and an anti-ovary antibody.    
     
     
         5 . The process according to  claim 4 , wherein the functional variant differs from said reference sequence by modification of the hydrocarbon residue of at least one amino acid of said reference sequence.  
     
     
         6 . The process according to  claim 5 , wherein the modification substantially conserves the hydrophilic or hydrophobic character of the hydrocarbon residue of the at least one amino acid.  
     
     
         7 . The process according to  claim 4 , wherein the oligopeptide comprises a sequence selected from the group consisting of SEQ ID NO: 1 to SEQ ID NO: 5.  
     
     
         8 . The process according to  claim 7 , wherein the oligopeptide consists of a sequence selected from the group consisting of SEQ ID NO: 1 to SEQ ID NO: 5.  
     
     
         9 . The process according to  claim 4 , wherein the biological sample is selected from the group consisting of blood serum, follicular liquid, peritoneal liquid, cervical mucus and saliva.  
     
     
         10 . The process according to  claim 4 , wherein the formation of an antigen-antibody complex is observed by an immunoenzymatic technique.  
     
     
         11 . The process according to  claim 4 , wherein said oligopeptide consists of FSH, a functional variant of FSH or the β-chain of FSH.  
     
     
         12 . The process according to  claim 4 , wherein said oligopeptide comprises a peptide sequence corresponding to the sequence of amino acids 78-93 of the β-chain of FSH.  
     
     
         13 - 20 . (canceled)  
     
     
         21 . The process according to  claim 4 , further comprising quantifying the amount of anti-ovary antibodies in the biological sample.  
     
     
         22 . The process according to  claim 4 , wherein the oligopeptide comprises SEQ ID NO: 5.  
     
     
         23 . The process according to  claim 22 , wherein the oligopeptide comprises a peptide sequence selected from the group consisting of SEQ ID NOs: 1-4.  
     
     
         24 . The process according to  claim 22 , comprising a disulfide bond between two cysteines of SEQ ID NO: 5.  
     
     
         25 . The process according to  claim 4 , wherein said oligopeptide comprises a peptide sequence Xaa1-Xaa2-Xaa3-Xaa4-Xaa5-Xaa6-Xaa7-Xaa8, wherein: 
 Xaa1 is NH 2 —CH(R1)COOH, where R1 is an oxygenated hydrocarbon radical;    Xaa2 is NH 2 —CH(R2)COOH, where R2 is an oxygenated and/or aminated hydrocarbon radical;    Xaa3 is NH 2 —CH(R3)COOH, where R3 is a sulfurated hydrocarbon radical;    Xaa4 is NH 2 —CH(R4)COOH, where R4 is an aminated hydrocarbon radical;    Xaa5 is NH 2 —CH(R5)COOH, where R5 is a sulfurated hydrocarbon radical;    Xaa6 is NH 2 —CH(R6)COOH, where R6 is a hydrocarbon radical;    Xaa7 is NH 2 —CH(R7)COOH, where R7 is an aminated hydrocarbon radical; and    Xaa8 is NH 2 —CH(R8)COOH, where R8 is a sulfurated hydrocarbon radical.    
     
     
         26 . The process according to  claim 25 , wherein: 
 Xaa1 is threonine or an amino acid having substantially the same hydrophilic or hydrophobic character of threonine;    Xaa2 is glutamine or an amino acid having substantially the same hydrophilic or hydrophobic character as glutamine;    Xaa3 is cysteine or an amino acid having substantially the same hydrophilic or hydrophobic character as cysteine;    Xaa4 is histidine or an amino acid having substantially the same hydrophilic or hydrophobic character as histidine;    Xaa5 is cysteine or an amino acid having substantially the same hydrophilic or hydrophobic character as cysteine;    Xaa6 is glycine or an amino acid having substantially the same hydrophilic or hydrophobic character as glycine;    Xaa7 is lysine or an amino acid having substantially the same hydrophilic or hydrophobic character as lysine; and    Xaa8 is cysteine or an amino acid having substantially the same hydrophilic or hydrophobic character as cysteine.    
     
     
         27 . The process according to  claim 4 , wherein said oligopeptide contains no more than 16 amino acids.

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