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
相关论文
共 50 条
  • [31] Ganglioside-Mediated Assembly of Amyloid ß-Protein: Roles in Alzheimer's Disease
    Matsuzaki, Katsumi
    Kato, Koichi
    Yanagisawa, Katsuhiko
    GANGLIOSIDES IN HEALTH AND DISEASE, 2018, 156 : 413 - 434
  • [32] Amyloid-β Oligomers: Possible Roles as Key Neurotoxins in Alzheimer's Disease
    Lublin, Alex L.
    Gandy, Sam
    MOUNT SINAI JOURNAL OF MEDICINE, 2010, 77 (01): : 43 - 49
  • [33] The roles of gold nanoparticles in the detection of amyloid-β peptide for Alzheimer's disease
    Zhao, Jiuhong
    Xu, Na
    Yang, Xiaotong
    Ling, Guixia
    Zhang, Peng
    COLLOID AND INTERFACE SCIENCE COMMUNICATIONS, 2022, 46
  • [34] The Role of Structural Polymorphism in Driving the Mechanical Performance of the Alzheimer's Beta Amyloid Fibrils
    Grasso, Gianvito
    Rebella, Martina
    Morbiducci, Umberto
    Tuszynski, Jack A.
    Danani, Andrea
    Deriu, Marco A.
    FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY, 2019, 7
  • [35] Impact of amyloid imaging on drug development in Alzheimer's disease
    Mathis, Chester A.
    Lopresti, Brian J.
    Klunk, William E.
    NUCLEAR MEDICINE AND BIOLOGY, 2007, 34 (07) : 809 - 822
  • [36] Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer's disease
    Reddy, P. Hemachandra
    EXPERIMENTAL NEUROLOGY, 2009, 218 (02) : 286 - 292
  • [37] Structural Analysis of Amylin and Amyloid β Peptide Signaling in Alzheimer's Disease
    Xie, Longsheng
    Lockhart, Christopher
    Bowers, Steven R.
    Klimov, Dmitri K.
    Jafri, Mohsin Saleet
    BIOMOLECULES, 2025, 15 (01)
  • [38] Abundant expression of zinc transporters in the amyloid plaques of Alzheimer's disease brain
    Zhang, Li-Hong
    Wang, Xin
    Stoltenberg, Meredin
    Danscher, Gorm
    Huang, Liping
    Wang, Zhan-You
    BRAIN RESEARCH BULLETIN, 2008, 77 (01) : 55 - 60
  • [39] Role of Interaction between Zinc and Amyloid Beta in Pathogenesis of Alzheimer’s Disease
    Sergey A. Kozin
    Biochemistry (Moscow), 2023, 88 : S75 - S87
  • [40] Role of Interaction between Zinc and Amyloid Beta in Pathogenesis of Alzheimer's Disease
    Kozin, Sergey A.
    BIOCHEMISTRY-MOSCOW, 2023, 88 (SUPPL 1) : S75 - S87
12345