Ladder-shaped polyether compound, desulfated yessotoxin, interacts with membrane-integral α-helix peptides

Megumi Mori, Tohru Oishi, Shigeru Matsuoka, Satoru Ujihara, Nobuaki Matsumori, Michio Murata, Masayuki Satake, Yasukatsu Oshima, Nobuto Matsushita, Saburo Aimoto

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Ladder-shaped polyether compounds, represented by brevetoxins, ciguatoxins, maitotoxin, and prymnesins, are thought to possess the high affinity to transmembrane proteins. As a model compound of ladder-shaped polyethers, we adopted desulfated yessotoxin (2) and examined its interaction with glycopholin A, a membrane protein known to form a dimer or oligomer. Desulfated yessotoxin turned out to interact with the α-helix so as to induce the dissociation of glycopholin oligomers when examined by SDS and PFO gel electrophoresis. The results provided the first evidence that lapper-shaped polyethers interact with transmembrane helix domains.

Original languageEnglish
Pages (from-to)5099-5103
Number of pages5
JournalBioorganic and Medicinal Chemistry
Volume13
Issue number17
DOIs
Publication statusPublished - Sep 1 2005
Externally publishedYes

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

Cite this