Journal
JOURNAL OF PEPTIDE SCIENCE
Volume 21, Issue 9, Pages 710-716Publisher
WILEY-BLACKWELL
DOI: 10.1002/psc.2795
Keywords
artificial functional peptide; cDNA display method; Helicobacter pylori; in vitro peptide evolution; vacuolating cytotoxin A
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Artificial peptides designed for molecular recognition of a bacterial toxin have been developed. Vacuolating cytotoxin A protein (VacA) is a major virulence factor of Helicobacter pylori, a gram-negative microaerophilic bacterium inhabiting the upper gastrointestinal tract, particularly the stomach. This study attempted to identify specific peptide sequences with high affinity for VacA using systematic directed evolution in vitro, a cDNA display method. A surface plasmon resonance-based biosensor and fluorescence correlation spectroscopy to examine binding of peptides with VacA identified a peptide (GRVNQRL) with high affinity. Cyclization of the peptide by attaching cysteine residues to both termini improved its binding affinity to VacA, with a dissociation constant (K-d) of 58nm. This study describes a new strategy for the development of artificial functional peptides, which are promising materials in biochemical analyses and medical applications. Copyright (c) 2015 European Peptide Society and John Wiley & Sons, Ltd.
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