Induction of lipid flip-flop by colicin E1 — a hallmark of proteolipidic pore formation in liposome membranes

The addition of the channel-forming domain of colicin E1 to liposomes elicited the transmembrane diffusion (flip-flop) of lipids concomitant to the release of the fluorescent dye from liposomes. Good correlation was found between kinetic and concentration dependences of the two processes. Both the l...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2010-06, Vol.75 (6), p.728-733
Main Authors: Sobko, A. A, Kovalchuk, S. I, Kotova, E. A, Antonenko, Y. N
Format: Article
Language:English
Subjects:
Analysis
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Colicins - metabolism
Diffusion
Fluorescent Dyes - metabolism
Hydrogen-Ion Concentration
Kinetics
Life Sciences
Lipids
Lipids - chemistry
Liposomes - metabolism
Membranes
Microbiology
Protein Binding
Spectrometry, Fluorescence
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Summary:The addition of the channel-forming domain of colicin E1 to liposomes elicited the transmembrane diffusion (flip-flop) of lipids concomitant to the release of the fluorescent dye from liposomes. Good correlation was found between kinetic and concentration dependences of the two processes. Both the liposome leakage and the lipid flip-flop were stimulated upon alkalinization of the buffer solution after colicin binding at acidic pH. These results in combination with the analysis of the data on colicin binding to liposomes provide evidence in favor of the validity of the toroidal (proteolipidic) pore model as the mechanism of colicin channel formation.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297910060076