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Direct visualization of solid ordered domains induced by polyene antibiotics in giant unilamellar vesicles
[Display omitted] •Nystatin makes domains in DOPC/Chol, DOPC/Chol/SM, and POPC but not in DOPC GUVs.•Amphotericin B and filipin form gel domains in pure POPC liposomes.•This ability correlates with the biological activity of the polyene antibiotics. Polyene antibiotics isolated from Streptomyces are...
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Published in: | Chemistry and physics of lipids 2014-10, Vol.183, p.204-207 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | [Display omitted]
•Nystatin makes domains in DOPC/Chol, DOPC/Chol/SM, and POPC but not in DOPC GUVs.•Amphotericin B and filipin form gel domains in pure POPC liposomes.•This ability correlates with the biological activity of the polyene antibiotics.
Polyene antibiotics isolated from Streptomyces are frequently used in treatment of mycoses. Confocal fluorescence microscopy has been employed to investigate the influence of polyene macrolide antibiotics nystatin, amphotericin B, and filipin on the phase separation in giant unilamellar vesicles. It has been demonstrated that nystatin produced the solid ordered domains in vesicles made from DOPC/Chol, DOPC/Chol/SM, and POPC while DOPC vesicles remained homogenous in the presence of polyene antibiotics. The ability of various polyenes to produce the solid ordered phase in POPC membranes has been compared. It has been shown that amphotericin B produced phase separation at lower concentration as compared with nystatin and filipin. Filipin was less effective in promotion of gel domains. The observed efficiency of polyene antibiotics to induce phase separation in lipid bilayers correlates with their biological activity. Present findings probably indicate the limitations of using of polyenes as fluorescence membrane probes for determination of strerol-enriched domains in plasma membrane of live cells. |
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ISSN: | 0009-3084 1873-2941 |
DOI: | 10.1016/j.chemphyslip.2014.07.008 |