Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers.

Abstract:

:The ionophore properties of magainin I, an antimicrobial and amphipathic peptide from the skin of Xenopus, were investigated in planar lipid bilayers. Circular dichroism studies, performed comparatively with alamethicin, in small or large unilamellar phospholipidic vesicles, point to a smaller proportion of alpha-helical conformation in membranes. A weakly voltage-dependent macroscopic conductance which is anion-selective is developed when using large aqueous peptide concentration with lipid bilayer under high voltages. Single-channel experiments revealed two main conductance levels occurring independently in separate trials. Pre-aggregates lying on the membrane surface at rest and drawn into the bilayer upon voltage application are assumed to account for this behaviour contrasting with the classical multistates displayed by alamethicin.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Duclohier H,Molle G,Spach G

doi

10.1016/S0006-3495(89)82746-8

subject

Has Abstract

pub_date

1989-11-01 00:00:00

pages

1017-21

issue

5

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(89)82746-8

journal_volume

56

pub_type

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