Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1564, Issue 2, Pages 359-364Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0005-2736(02)00470-4
Keywords
amphipathy; pore-forming; alpha helix; skin mucus; fish
Categories
Ask authors/readers for more resources
Pleurocidin, a 25-residue alpha helical cationic peptide, isolated from skin mucous secretions of the winter flounder, displays a strong antimicrobial activity and appears to play a role in innate host defence. This peptide would be responsible for pore formation in the membrane of bacteria leading to lysis and therefore death. In this study, we investigated the behaviour of pleurocidin in different planar lipid bilayers to determine its mechanism of membrane permeabilisation. Macroscopic conductance experiments showed that pleurocidin did not display a pore-forming activity in neutral phosphatidylcholine/phosphatidylethanolamine (POPE) lipid bilayers. However, in 73:1 PC/PE/ phosphatidylserine (PS) lipid bilayers, pleurocidin showed reproducible I/V curves at different peptide concentrations. This activity is confirmed by single-channel experiments since well-defined ion channels were obtained if the lipid mixture was containing an anionic lipid (PS). The ion channel characteristics such as-no voltage dependence, only one unitary conductance, linear relation ship current-voltage-, are not in favour of the membrane permeabilisation according to the barrel model but rather by the toroidal pore formation. (C) 2002 Elsevier Science B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available