Identification and synthesis of altered peptides modulating T cell recognition of a synthetic peptide antigen.

Abstract

In studies of T cell responses to synthetic peptides we have observed agonist and antagonist activities associated with contaminants identified within the parent synthesis. The synthesis of two candidate analogues implied by a peptide contaminant formed during the synthesis of La 51-58 (IMIKFNRL) has been carried out. The peptide contaminant was 17-18 Da smaller than the parent peptide consistent with a modified asparagine residue at position 6 and so we synthesised both an aspartimide and a nitrile analogue, representing cyclisation or dehydration of the asparagine residue. The candidate aspartimide and nitrile analogues both bound empty MHC class I molecules to form allo determinants recognised by monoclonal antibodies. These results demonstrate that altered synthetic peptides can bind class I MHC molecules and prompt caution in the use of synthetic peptides as a source of immunising antigen.

• Authors: N J Ede, W Chen, J McCluskey, D C Jackson, A W Purcell
• Journal: Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity (Biomed Pept Proteins Nucleic Acids) Vol. 1 Issue 4 Pg. 231-4 ( 1995) ISSN: 1353-8616 [Print] England
• PMID: 9346837 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• H-2 Antigens
• H-2Kb protein, mouse
• Indicators and Reagents
• Nitriles
• Oligopeptides
• Aspartic Acid
• aspartimide

Topics

• Amino Acid Sequence
• Animals
• Aspartic Acid (analogs & derivatives)
• Cell Line
• H-2 Antigens (immunology)
• Indicators and Reagents
• Mice
• Nitriles
• Oligopeptides (chemical synthesis, chemistry, immunology)
• T-Lymphocytes, Cytotoxic (immunology)