Conformation and location of membrane-bound salinomycin-sodium complex deduced from NMR in isotropic bicelles.

Conformation and location of membrane-bound salinomycin-sodium complex deduced from NMR in isotropic bicelles. Research Abstract Details 

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Conformation and location of membrane-bound salinomycin-sodium complex deduced from NMR in isotropic bicelles. Abstract Text:

Nobuaki Matsumori,Atsushi Morooka,Michio Murata,Nobuaki Matsumori,Atsushi Morooka,Michio Murata,Nobuaki Matsumori,Atsushi Morooka,Michio Murata,

An ionophore antibiotic salinomycin was studied in a membrane environment consisting of isotropic bicelles, a better model for biological membranes than micelles, and its conformation and topological orientation in bicelles was determined. 2D NMR measurements and restrained conformational search revealed that salinomycin-sodium salt in bicelles adopts an open conformation in which the orientation of the E-ring is significantly different from that in crystal and solution structures. This conformational alteration breaks an intramolecular hydrogen bond between 28-OH and 1-O, dislocates the ether oxygen of the E-ring from a coordinated position to the sodium ion observed in the crystal, and consequently weakens the complexation between salinomycin and the sodium ion. Paramagnetic relaxation experiments using doxyl-phospholipids reveal that salinomycin is embedded shallowly in bicelles, with both terminals being closer to the water interface and the olefin portion facing the bicelle interior. Measurements of intermolecular NOEs between salinomycin and phospholipids further supported this orientation. Weaker complexation with sodium ion and positional preference in the membrane polar region may facilitate the catch-and-release of metal ions at the polar/nonpolar interface of bilayers. On the basis of these findings, a model for salinomycin-assisted transport of metal ions across biological membranes is proposed.

Conformation and location of membrane-bound salinomycin-sodium complex deduced from NMR in isotropic bicelles. Publishing Authors By Initials

N Matsumori,A Morooka,M Murata,N Matsumori,A Morooka,M Murata,N Matsumori,A Morooka,M Murata,

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Conformation and location of membrane-bound salinomycin-sodium complex deduced from NMR in isotropic bicelles. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of the American Chemical Society

VOLUME: 129

Page Numbers: 14989-95

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 10

MONTH: 11

YEAR: 2007

Conformation and location of membrane-bound salinomycin-sodium complex deduced from NMR in isotropic bicelles. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Conformation and location of membrane-bound salinomycin-sodium complex deduced from NMR in isotropic bicelles.

AFFILIATION: Contribution from the Department of Chemistry, Graduate School of Science, Osaka University, Machikaneyama, Toyonaka, Osaka 560-0043, Japan.

Country: United States

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MEDLINETA: J Am Chem Soc

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