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Cyclic peptides selected by phage display mimic the natural epitope recognized by a monoclonal anti-colicin A antibody

✍ Scribed by Stephane Coulon; Jean-Yves Metais; Martine Chartier; Jean-Paul Briand; Dr Daniel Baty

Book ID: 105360386
Publisher: John Wiley and Sons
Year: 2004
Tongue: English
Weight: 162 KB
Volume: 10
Category: Article
ISSN: 1075-2617
DOI: 10.1002/psc.574

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✦ Synopsis

Abstract

A 10‐mer random peptide library displayed on filamentous bacteriophage was used to determine the molecular basis of the interaction between the monoclonal anti‐colicin A antibody 1C11 and its cognate epitope. Previous studies established that the putative epitope recognized by 1C11 antibody is composed of amino acid residues 19–25 (RGSGPEP) of colicin A. Using the phage display technique it was confirmed that the epitope of 1C11 antibody was indeed restricted to residues 19–25 and the consensus motif RXXXPEP was identified. Shorter consensus sequences (RXXPEP, RXXEP, KXXEP) were also selected. It was also demonstrated that the disulfide bond found in one group of the selected peptides was crucial for 1C11 antibody recognition. It was shown that cyclization of the peptides by disulfide bond formation could result in a structure that mimics the natural epitope of colicin A. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.

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