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 Jjournal_title
Biophysical journalauthors
Duclohier H,Molle G,Spach Gdoi
10.1016/S0006-3495(89)82746-8subject
Has Abstractpub_date
1989-11-01 00:00:00pages
1017-21issue
5eissn
0006-3495issn
1542-0086pii
S0006-3495(89)82746-8journal_volume
56pub_type
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