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Interaction of rifabutin with model membranes
Liposomal and free rifabutin were separated by the method of gel filtration. The percents of rifabutin bound to liposomes of different phospholipid composition were measured. The presence of negatively charged phospholipids increased the degree of binding. Binding decreased with increasing the ionic...
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Published in: | Bulletin of experimental biology and medicine 2005-12, Vol.140 (6), p.711-713 |
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creator | Shakina, Yu N Vostrikov, V V Sorokoumova, G M Selishcheva, A A Shvets, V I |
description | Liposomal and free rifabutin were separated by the method of gel filtration. The percents of rifabutin bound to liposomes of different phospholipid composition were measured. The presence of negatively charged phospholipids increased the degree of binding. Binding decreased with increasing the ionic strength. Incubation of rifabutin with liposomes containing anthryl phosphatidylcholine was accompanied by fluorescence quenching. Activity of rifabutin depended on the phospholipid composition of liposomes. Our results indicate that binding of rifabutin is associated with electrostatic and hydrophobic interactions. |
doi_str_mv | 10.1007/s10517-006-0062-y |
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subjects | Adsorption Animals Antibiotics, Antitubercular - pharmacology Chromatography, Gel Ions Lipid Bilayers - metabolism Liposomes - chemistry Membranes - chemistry Phosphatidylcholines - chemistry Protein Binding Rifabutin - chemistry Rifabutin - pharmacology Spectrometry, Fluorescence Static Electricity |
title | Interaction of rifabutin with model membranes |
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