Structure of Membrane-Bound Amphidinol 3 in Isotropic Small Bicelles

Amphidinol 3 (AM3) exhibits a potent membrane permeabilizing activity by forming pores in biological membranes. We examined the conformation and location of AM3 using isotropic bicelles, a more natural membrane model than micelles. The results show that AM3 takes turn structures at the two tetrahydr...

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Veröffentlicht in:Organic letters 2008-10, Vol.10 (19), p.4191-4194
Hauptverfasser: Houdai, Toshihiro, Matsumori, Nobuaki, Murata, Michio
Format: Artikel
Sprache:eng
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Zusammenfassung:Amphidinol 3 (AM3) exhibits a potent membrane permeabilizing activity by forming pores in biological membranes. We examined the conformation and location of AM3 using isotropic bicelles, a more natural membrane model than micelles. The results show that AM3 takes turn structures at the two tetrahydropyran rings. Most of the hydrophilic region of the molecule is predominantly present in the surface, while the hydrophobic polyolefin penetrates in the bicelle interior.
ISSN:1523-7060
1523-7052
DOI:10.1021/ol8016337