非洲爪蟾皮肤中的抗菌肽马盖宁I在平面脂质双分子层中形成阴离子通透通道。
Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers.
作者信息
Duclohier H, Molle G, Spach G
机构信息
UA 500 CNRS, Faculté des Sciences de Rouen, Mont Saint-Aignan, France.
出版信息
Biophys J. 1989 Nov;56(5):1017-21. doi: 10.1016/S0006-3495(89)82746-8.
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.
摘要
对非洲爪蟾皮肤中的抗菌两亲性肽马盖宁I在平面脂质双分子层中的离子载体特性进行了研究。在小的或大的单层磷脂囊泡中与短杆菌肽A进行比较的圆二色性研究表明，在膜中α-螺旋构象的比例较小。当在高电压下使用高浓度的水性肽与脂质双分子层时，会产生一种弱电压依赖性的宏观电导，该电导具有阴离子选择性。单通道实验揭示了在单独试验中独立出现的两个主要电导水平。静止时位于膜表面并在施加电压时被吸入双分子层的预聚集体被认为是造成这种行为的原因，这与短杆菌肽A所显示的经典多状态形成对比。
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