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

N. J. Ede, W. Chen, J. McCluskey, D. C. Jackson, A. W. Purcell

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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.

Original languageEnglish
Pages (from-to)231-234
Number of pages4
JournalBiomedical Peptides, Proteins & Nucleic Acids: Structure, Synthesis & Biological Activity
Volume1
Issue number4
Publication statusPublished - 1 Jan 1995
Externally publishedYes

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