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• W2156820656 endingPage "3799" @default.
• W2156820656 startingPage "3795" @default.
• W2156820656 abstract "The interactions of filipin III, amphotericin B, nystatin, and lagosin with sterols in aqueous suspension and in vesicles were followed by fluorescence excitation spectra and by measurement of polarized fluorescence intensities. The equilibrium constants for association of the polyene antibiotics with aqueous suspensions of cholesterol follow the order filipin III > amphotericin B > nystatin > lagosin, in agreement with the order reported for the extent of damage these antibiotics cause in natural and model membranes. Fluorescence polarization measurements show that hydrophobic forces are primarily responsible for the formation of the complexes. Filipin III undergoes a large enhancement in fluorescence polarization on binding to aqueous suspensions of cholesterol and epi-cholesterol, and to vesicles of lecithin-cholesterol, lecithin-beta-cholestanol, and lecithinergosterol. Small increases in polarization occur on interaction of filipin III with vesicles derived from lecithin and epi-cholesterol, thiocholesterol, and androstan-3beta-ol. Amphotericin B undergoes a relatively constant enhancement in fluorescence polarization on interaction with the various lecithin-sterol vesicles used and does not display the selectivity exhibited by filipin III. It is suggested that filipin III serves as a probe of lecithin-sterol interaction." @default.
• W2156820656 created "2016-06-24" @default.
• W2156820656 creator A5004530946 @default.
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• W2156820656 date "1972-12-01" @default.
• W2156820656 modified "2023-09-27" @default.
• W2156820656 title "Fluorescence Studies of the Binding of the Polyene Antibiotics Filipin III, Amphotericin B, Nystatin, and Lagosin to Cholesterol" @default.
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• W2156820656 doi "https://doi.org/10.1073/pnas.69.12.3795" @default.
• W2156820656 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/389875" @default.
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