Abstract
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.
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