Structure and function of oligosaccharide-binding peptides that selected from random libraries

Teruhiko Matsubara, Kazutoshi Iijima, Machiko Sumi, Toshinori Sato

Research output: Contribution to conferencePaperpeer-review

Abstract

The peptides that bind to oligosaccharide of glycolipid were identified and their function was assayed. The monolayers of ganglioside were employed for an affinity selection by phage-displayed random libraries, and the ganglioside-binding peptides were selected. A synthetic peptide p3 inhibited the cholera toxin binding to GM1 (Galβ1-3GalNAcβ1-4(Neu5Acα2-3) Galβ1-4Glcβ1-1′Cer) with IC50 of 1 μM. A raft-like hybrid lipid bilayer was prepared and the binding of the peptide were visualized by atomic force microscopy, indicated that the peptide was specific to glycocluster in the lipid membrane. Furthermore, GM3 (Neu5Acα2- 3Galβ1-4Glcβ1-1′′Cer)-binding peptides bound to cells and the corresponding N-stearoyl derivatives inhibited the infection of Madin-Darby canine kidney cells by influenza virus, which recognizes α2,3- and α2,6-linked sialylgalactose structures.

Original languageEnglish
Pages5221-5222
Number of pages2
Publication statusPublished - 2006 Dec 1
Event55th Society of Polymer Science Japan Symposium on Macromolecules - Toyama, Japan
Duration: 2006 Sep 202006 Sep 22

Other

Other55th Society of Polymer Science Japan Symposium on Macromolecules
CountryJapan
CityToyama
Period06/9/2006/9/22

Keywords

  • Atomic force microscopy
  • Cluster
  • Glycolipid
  • Peptide library
  • Phage display
  • Sugar recognition

ASJC Scopus subject areas

  • Engineering(all)

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