Complementary DNA display selection of high‐affinity peptides binding the vacuolating toxin (VacA) of Helicobacter pylori |
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| Authors: | Yumiko Hayakawa Mitsuhiro Matsuno Makoto Tanaka Akihiro Wada Koichiro Kitamura Osamu Takei Ryuzo Sasaki Tamio Mizukami Makoto Hasegawa |
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| Affiliation: | 1. Graduate School of Bioscience, Nagahama Institute of Bio‐Science and Technology, Shiga, Japan;2. Institute for Tropical Medicine, Nagasaki University, Nagasaki, Japan;3. JANUSYS Co., Ltd., Saitama, Japan;4. Lifetech Co., Ltd., Saitama, Japan |
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| Abstract: | 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 (Kd) of 58 nm . This study describes a new strategy for the development of artificial functional peptides, which are promising materials in biochemical analyses and medical applications. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd. |
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| Keywords: | artificial functional peptide cDNA display method Helicobacter pylori in vitro peptide evolution vacuolating cytotoxin A |
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