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Issue 23, 2010
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Design, synthesis and evaluation of β-lactam antigenic peptide hybrids; unusual opening of the β-lactam ring in acidic media

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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

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Supplementary files

Article information


Submitted
05 Mar 2010
Accepted
02 Sep 2010
First published
07 Oct 2010

Org. Biomol. Chem., 2010,8, 5345-5353
Article type
Paper

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

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