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阴离子脂质对β-淀粉样肽在膜上的重组作用影响很小。

Anionic lipids modulate little the reorganization effect of amyloid-beta peptides on membranes.

作者信息

Ivankov Oleksandr, Badreeva Dina R, Ermakova Elena V, Kondela Tomáš, Murugova Tatiana N, Kučerka Norbert

机构信息

Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research, Dubna, Russia.

出版信息

Gen Physiol Biophys. 2023 Jan;42(1):59-66. doi: 10.4149/gpb_2022052.

DOI:10.4149/gpb_2022052
PMID:36705305
Abstract

Amyloid-β peptide interactions with model lipid membranes have been studied by means of small angle neutron scattering and molecular dynamics simulations. These interactions had been indicated recently as an origin of the membrane structure reorganizations between spherical small unilamellar vesicles and planar bicelle-like structures. In present work, we investigate the influence of charge on the peptide-triggered morphological changes by introducing the anionic lipid DMPS to the underlying DMPC membrane. Changes to the membrane thickness and the overall membrane structure with and without Aβ25-35 incorporated have been investigated over a wide range of temperatures. Our results document the previously reported morphological reformations between bicelle-like structures present in gel phase and small unilamellar vesicles present in fluid phase to be independent from the charge existence in the system.

摘要

通过小角中子散射和分子动力学模拟研究了淀粉样β肽与模型脂质膜的相互作用。最近表明,这些相互作用是球形小单层囊泡和平面双分子层样结构之间膜结构重组的起源。在本研究中,我们通过将阴离子脂质DMPS引入下层DMPC膜来研究电荷对肽引发的形态变化的影响。在很宽的温度范围内,研究了掺入和未掺入Aβ25-35时膜厚度和整体膜结构的变化。我们的结果证明,先前报道的凝胶相中存在的双分子层样结构与液相中存在的小单层囊泡之间的形态重构与系统中电荷的存在无关。

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