Journal
FEBS LETTERS
Volume 576, Issue 1-2, Pages 205-210Publisher
WILEY
DOI: 10.1016/j.febslet.2004.09.016
Keywords
bilayer lipid membrane; spontaneous curvature; ion channel; toroidal pore; colicin E1; trans-membrane current; dye eakage; tryptophan fluorescence
Funding
- FIC NIH HHS [TW01235] Funding Source: Medline
- NIGMS NIH HHS [GM-18457] Funding Source: Medline
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The channel activity of colicin E1 was studied in planar lipid bilayers and liposomes. Colicin E1 pore-forming activity was found to depend on the curvature of the lipid bilayer, as judged by the effect on channel activity of curvature-modulating agents. In particular, the colicin-induced trans-membrane current was augmented by lysophosphatidylcholine reduced by, oleic acid, agents promoting positive and negative membrane curvature, respectively. The data obtained imply direct involvement of lipids in the formation of colicin E1-induced pore walls. It is inferred that the toroidal pore model previously validated for small antimicrobial peptides is applicable to colicin E1, a large protein that contains ten alpha-helices in its pore-forming domain. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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