Roles of zinc ions and structural polymorphism of β-amyloid in the development of Alzheimer's disease

被引：24
作者：
Kulikova, A. A. [1 ]
Makarov, A. A. [1 ]
Kozin, S. A. [1 ]
机构：
[1] Russian Acad Sci, VA Engelhardt Mol Biol Inst, Moscow 119991, Russia
来源：
MOLECULAR BIOLOGY | 2015年 / 49卷 / 02期
关键词：
Alzheimer's disease; beta-amyloid; zinc; aggregation; oligomerization; dimerization; structural polymorphism; metal-binding domain; posttranslational modification; mutations; IMPAIR SYNAPTIC PLASTICITY; A-BETA; PRECURSOR PROTEIN; POSTTRANSLATIONAL MODIFICATIONS; BINDING-SITE; NEURODEGENERATIVE DISORDERS; TRANSMEMBRANE DOMAIN; OLIGOMER FORMATION; SOLUBLE OLIGOMERS; NATURAL OLIGOMERS;
D O I：
10.1134/S0026893315020065
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：
Aggregation of the beta-amyloid peptide (A beta) underlies the development of Alzheimer's disease. The review considers the main steps of the A beta formation and aggregation. Emphasis is placed on the interaction of zinc ions with the metal-binding domain 1-16 of A beta as a molecular mechanism leading to A beta aggregation. Recent studies of native modifications in the A beta metal-binding domain revealed its structural polymorphism. The prospects of further studying the modifications to determine the pathogenetic mechanism of A beta aggregation are discussed.
引用
收藏
页码：217 / 230
页数：14
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