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

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.

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.Figure optionsDownload as PowerPoint slide