Vol 49(2015) N 2 p. 217-230; DOI 10.1134/S0026893315020065
A.A. Kulikova, A.A. Makarov, S.A. Kozin*
Roles of zinc ions and structural polymorphism of β-amyloid in the development of Alzheimer's diseaseEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia
Received - 2014-11-17; Accepted - 2014-11-17
Aggregation of the β-amyloid peptide (Aβ) underlies the development of Alzheimer's disease. The review considers the main steps of the Aβ formation and aggregation. Emphasis is placed on the interaction of zinc ions with the metal-binding domain 1-16 of Aβ as a molecular mechanism leading to Aβ aggregation. Recent studies of native modifications in the Aβ metal-binding domain revealed its structural polymorphism. The prospects of further studying the modifications to determine the pathogenetic mechanism of Aβ aggregation are discussed.
Alzheimer's disease, β-amyloid, zinc, aggregation, oligomerization, dimerization, structural polymorphism, metal-binding domain, posttranslational modification, mutations