Peptides binding to a Gb3 mimic selected from a phage library

被引:20
作者
Miura, Y [1 ]
Sasao, Y
Kamihira, M
Sakaki, A
Iijima, S
Kobayashi, K
机构
[1] Nagoya Univ, Grad Sch Engn, Dept Mol Design & Engn, Chikusa Ku, Nagoya, Aichi 4648603, Japan
[2] Nagoya Univ, Grad Sch Engn, Dept Biotechnol, Chikusa Ku, Nagoya, Aichi 4648603, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 2004年 / 1673卷 / 03期
关键词
phage display peptide library; protein-oligosaccharide interaction; Gb3; Shiga toxin; quartz crystal microbalance;
D O I
10.1016/j.bbagen.2004.04.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Peptides binding to a Gb3 mimic were selected from 12-mer peptide library. The self-assembled monolayer (SAM) of a Gb3 mimic was formed on the gold surface, and biopanning was carried out with the phage display peptide library. After three rounds of biopanning, four individual sequences were obtained from 10 phage clones, and the selected peptides having the specific 7-mer sequence (FHENWPS) showed affinities to the Gb3 mimic as strong as to RCA(120). Molecular dynamics calculations suggested that the peptides bound to the Gb3 mimic by hydrophobic interaction and hydrogen bonding formation, and the cooperative interactions played an important role in the recognition. The Stx-1 binding was inhibited by the peptides. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:131 / 138
页数:8
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