TY - JOUR
T1 - Ladder-shaped polyether compound, desulfated yessotoxin, interacts with membrane-integral α-helix peptides
AU - Mori, Megumi
AU - Oishi, Tohru
AU - Matsuoka, Shigeru
AU - Ujihara, Satoru
AU - Matsumori, Nobuaki
AU - Murata, Michio
AU - Satake, Masayuki
AU - Oshima, Yasukatsu
AU - Matsushita, Nobuto
AU - Aimoto, Saburo
N1 - Funding Information:
We are grateful to Professor Koji Nakanishi for continuous encouragements and generous gift of brevetoxins; to Dr. Toshihiro Hohdai, Saori Seki, and Nagy Morsy for their help in dinoflagellate culture. This study was supported by Nagase Science and Technology Foundation, and by a Grant-in-Aid for Scientific Research on Priority Area ‘Creation of Biologically Functional Molecules’ from MEXT Japan.
PY - 2005/9/1
Y1 - 2005/9/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.bmc.2005.05.039
DO - 10.1016/j.bmc.2005.05.039
M3 - Article
C2 - 15990315
AN - SCOPUS:22844434675
VL - 13
SP - 5099
EP - 5103
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
SN - 0968-0896
IS - 17
ER -