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

A ladder-shaped polyether compound, desulfated yessotoxin, markedly enhanced the dissociation of oligomers of glycopholin A and its transmembrane peptide (GpA-TM) into dimers and monomers. Ladder-shaped polyether compounds, represented by brevetoxins, ciguatoxins, maitotoxin, and prymnesins, are tho...

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Published in:Bioorganic & medicinal chemistry 2005-09, Vol.13 (17), p.5099-5103
Main Authors: Mori, Megumi, Oishi, Tohru, Matsuoka, Shigeru, Ujihara, Satoru, Matsumori, Nobuaki, Murata, Michio, Satake, Masayuki, Oshima, Yasukatsu, Matsushita, Nobuto, Aimoto, Saburo
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Electrophoresis, Polyacrylamide Gel
Ethers, Cyclic - chemistry
Glycopholin
Glycophorin - chemistry
Hemolysis
Ladder-shaped polyether
Membrane Proteins - chemistry
Molecular Sequence Data
Oxocins - chemistry
Peptides - chemistry
Transmembrane peptides
Yessotoxin
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Summary:A ladder-shaped polyether compound, desulfated yessotoxin, markedly enhanced the dissociation of oligomers of glycopholin A and its transmembrane peptide (GpA-TM) into dimers and monomers. 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.
ISSN:0968-0896
1464-3391
DOI:10.1016/j.bmc.2005.05.039