Interactions between amyloid β peptide and lipid membranes

被引：84
|
作者：
Niu, Zheng [1 ,2 ]
Zhang, Zhengfeng [1 ]
Zhao, Weijing [1 ]
Yang, Jun [1 ]
机构：
[1] Chinese Acad Sci, Key Lab Magnet Resonance Biol Syst, State Key Lab Magnet Resonance & Atom & Mol Phys, Wuhan Ctr Magnet Resonance,Wuhan Inst Phys & Math, Wuhan 430071, Hubei, Peoples R China
[2] Tech Univ Munich, Dept Chem, D-85748 Garching, Germany
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2018年 / 1860卷 / 09期
基金：
中国国家自然科学基金;
关键词：
Alzheimer's disease; beta-Amyloid peptide; Fibrillation; Phospholipids; Membrane disruption; Solid-state nuclear magnetic resonance; ALZHEIMERS-DISEASE; A-BETA; METAL-IONS; GANGLIOSIDE CLUSTERS; SECONDARY NUCLEATION; PROTEIN AGGREGATION; MECHANISTIC INSIGHT; MOLECULAR-STRUCTURE; CHANNEL FORMATION; FIBRIL FORMATION;
D O I：
10.1016/j.bbamem.2018.04.004
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The presence of amyloid plaques in the brain is a typical characteristic of Alzheimer's disease (AD). Amyloid plaques are formed from the deposits of aggregated amyloid beta peptide (A beta). The toxicity induced by A beta aggregates is correlated with A beta-membrane interactions. The mutual influences between aggregation and membranes are complicated and unclear. In recent years advanced experiments and findings are emerging to give us more detailed information on A beta-membrane interactions. In this review, we mainly focus on the A beta-membrane interactions and membrane-induced A beta structures. The mechanism of A beta-membrane interactions is also summarized, which provides insights into the prevention and treatment of AD.
引用
收藏
页码：1663 / 1669
页数：7
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