Physicochernical interactions of arnyloid-peptide with lipid bilayers

被引:170
|
作者
Matsuzaki, Katsumi [1 ]
机构
[1] Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2007年 / 1768卷 / 08期
关键词
Alzheimer's disease; amyloid beta-peptide; lipid bilayer; lipid raft; ganglioside; fibril formation;
D O I
10.1016/j.bbamem.2007.02.009
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 aggregation and deposition onto neuronal cells of amyloid beta-peptide (A beta) is central to the pathogenesis of Alzheimer's disease. Accumulating evidence suggests that membranes play a catalytic role in the aggregation of A. This article summarizes the structures and properties of A beta in solution and the physicochemical interaction of A with lipid bilayers of various compositions. Reasons for discrepancies between results by different research groups are discussed. The importance of ganglioside clusters in the aggregation of A is emphasized. Finally, a hypothetical physicochemical cascade in the pathogenesis of the disease is proposed. (c) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:1935 / 1942
页数:8
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