Specific binding of GM1-binding peptides to high-density GM1 in lipid membranes

Teruhiko Matsubara, Kazutoshi Iijima, Miwa Nakamura, Takao Taki, Yoshio Okahata, Toshinori Sato

研究成果: Article査読

17 被引用数 (Scopus)

抄録

The ganglioside Galβ1-3GalNAcβ1-4(Neu5Acα2-3)Galβ1- 4Glcβ1-1′Cer (GM1) is an important receptor. We have previously identified GM1-binding peptides based on affinity selection from a random peptide library. In the present study, we determined the amino acids essential for binding GM1 and investigated the specific interaction with GM1 in the lipid membrane. Arginines and aromatic amino acids in the consensus sequence (W/F)RxL(xP/Px)xFxx(Rx/xR)xP contributed to the ability of the peptides to bind GM1. The peptide p3, VWRLLAPPFSNRLLP, having the consensus sequence, showed high affinity for GM1 with a dissociation constant of 1.2 μM. Furthermore, the density-dependent binding of p3 was investigated using mixed monolayers of GM1 and Glcβl-1′Cer (GlcCer). p3 binds preferentially to high-density GM1, and its interaction with GM1 was found to be cooperative based on a Hill plot. These results indicated that a lateral assembly of GM1 molecules was required for the recognition of carbohydrates by p3. The GM1-binding peptide played a role as a unique anti-GM1 probe differing from the cholera toxin B subunit or antibodies.

本文言語English
ページ(範囲)708-714
ページ数7
ジャーナルLangmuir
23
2
DOI
出版ステータスPublished - 2007 1 16

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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