Ladder-shaped polyether compound, desulfated yessotoxin, interacts with membrane-integral alpha-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 alpha-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 ladder-shaped polyethers interact with transmembrane helix domains.
Mori
Megumi
M
Department of Chemistry Graduate School of Science, Osaka University Toyonaka, Osaka 560-0043, Japan.
Oishi
Tohru
T
Matsuoka
Shigeru
S
Ujihara
Satoru
S
Matsumori
Nobuaki
N
Murata
Michio
M
Satake
Masayuki
M
Oshima
Yasukatsu
Y
Matsushita
Nobuto
N
Aimoto
Saburo
S
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D004988:Ethers, Cyclic / Q000737:chemistry*; D006021:Glycophorins / Q000737:chemistry; D006461:Hemolysis; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D008978:Mollusk Venoms; D035964:Oxocins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*
D004988:Ethers, Cyclic; D006021:Glycophorins; D008565:Membrane Proteins; D008978:Mollusk Venoms; D035964:Oxocins; D010455:Peptides; C066632:yessotoxin