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. 1989 Nov;56(5):1017–1021. doi: 10.1016/S0006-3495(89)82746-8

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

H Duclohier 1, G Molle 1, G Spach 1
PMCID: PMC1280599  PMID: 2481510

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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