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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Bibliographic Details
Published in:Bulletin of experimental biology and medicine 2005-12, Vol.140 (6), p.711-713
Main Authors: Shakina, Yu N, Vostrikov, V V, Sorokoumova, G M, Selishcheva, A A, Shvets, V I
Format: Article
Language:English
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
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Summary: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.
ISSN:0007-4888
1573-8221
DOI:10.1007/s10517-006-0062-y