title: [The role of zinc ions and structural polymorphism of β-amyloid in the Alzheimer's disease initiation].
abstract: Aggregation of β-amyloid peptide (Aβ) underlies the development of Alzheimer's disease. Here we review the main stages of Aβ formation and aggregation. We highlight the importance of interaction of zinc ions with the metal-binding domain 1-16 of Aβ as a molecular mechanism that leads to Aβ aggregation. We analyze recent studies of the native modifications of the Aβ metal-binding domain that determine its structural polymorphism. The prospects for further studies of these modifications aimed at revealing the pathogenic mechanism of Aβ aggregation are discussed.
authors.forename: A A
authors.initials: AA
authors.lastname: Kulikova
authors.forename: A A
authors.initials: AA
authors.lastname: Makarov
authors.forename: S A
authors.initials: SA
authors.lastname: Kozin
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D000818:Animals; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism*; D066263:Protein Aggregation, Pathological / Q000378:metabolism* / Q000473:pathology; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D015032:Zinc / Q000378:metabolism*
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C433241:amyloid beta-protein (1-16); D015032:Zinc