Jump to main content
Jump to site search

Issue 23, 2010
Previous Article Next Article

Design, synthesis and evaluation of β-lactam antigenic peptide hybrids; unusual opening of the β-lactam ring in acidic media

Author affiliations

Abstract

β-Lactam peptides were envisioned as conformational constraints in antigenic peptides (APs). Three different β-lactam tripeptides of varying flexibility were prepared in solution and incorporated in place of the central part of the altered melanoma associated antigenic peptide Leu27-Melan-A26–35 using solid phase synthesis techniques. Upon TFA cleavage from the solid support, an unexpected opening of the β-lactam ring occurred with conservation of the amide bond. After adaptation of the solid phase synthesis strategy, β-lactam peptides were successfully obtained and both opened and closed forms were evaluated for their capacity to bind to the antigen-presenting class-I MHC HLA-A2 protein system. None of the closed β-lactam peptides bound to HLA-A2, but their opened variants were shown to be moderate to good HLA-A2 ligands, one of them being even capable of stimulating a Melan-A-specific T cell line.

Graphical abstract: Design, synthesis and evaluation of β-lactam antigenic peptide hybrids; unusual opening of the β-lactam ring in acidic media

Back to tab navigation

Supplementary files

Publication details

The article was received on 05 Mar 2010, accepted on 02 Sep 2010 and first published on 07 Oct 2010


Article type: Paper
DOI: 10.1039/C003877F
Citation: Org. Biomol. Chem., 2010,8, 5345-5353
  •   Request permissions

    Design, synthesis and evaluation of β-lactam antigenic peptide hybrids; unusual opening of the β-lactam ring in acidic media

    M. Tarbe, I. Azcune, E. Balentová, J. J. Miles, E. E. Edwards, K. M. Miles, P. Do, B. M. Baker, A. K. Sewell, J. M. Aizpurua, C. Douat-Casassus and S. Quideau, Org. Biomol. Chem., 2010, 8, 5345
    DOI: 10.1039/C003877F

Search articles by author

Spotlight

Advertisements