Peptides binding to a Gb3 mimic selected from a phage library

• Miura, Yoshiko

• Sasao, Yuuki

• Kamihira, Masamichi

• Sakaki, Akio

• Iijima, Shinji

• Kobayashi, Kazukiyo

Abstract

Peptides binding to a Gb3 mimic were selected from 12mer 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 3 rounds of biopanning, four individual sequences were obtained from 10 phage clones, and the selected peptides having the specific 7mer 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.

identifier:https://dspace.jaist.ac.jp/dspace/handle/10119/4945

Journal

• Biochimica et Biophysica Acta (BBA) : General Subjects

  Biochimica et Biophysica Acta (BBA) : General Subjects 1673 (3), 131-138, 2004-08-04

  Elsevier

Keywords

• phage display peptide library
• protein-oligosaccharide interaction
• Gb3
• Shiga toxin
• quartz crystal microbalance

Details

• CRID: 1050282812513908096
• NII Article ID: 120000861716
• ISSN: 03044165
• Web Site: http://hdl.handle.net/10119/4945
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • CiNii Articles