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The inhibitory mechanism of copper(Ⅱ) on the aggregation of amyloid β-peptide (Aβ) was investigated by molecular dynamics simulations.The bindingmode ofcopper(Ⅱ) with Aβ is characterized by the imidazolenitrogenatom,Nπ, of the histidine residue H13,acting as the anchoring site, and the backbone’s deprotoned amide nitrogen atoms as the main binding sites. Drove by the coordination bonds and their induced hydrogen bond net, the conformations of Aβ converted from β-sheet non-β-sheet conformations, which destabilized the aggregation of Aβ into fibrils.
The inhibitory mechanism of copper (Ⅱ) on the aggregation of amyloid β-peptide (Aβ) was investigated by molecular dynamics simulations. The binding mode of copper (Ⅱ) with Aβ is characterized by the imidazolenitrogenatom, Nπ, of the histidine residue H13, acting as the anchoring site, and the backbone’s deprotoned amide nitrogen atoms as the main binding sites. Drove by the coordination bonds and their induced hydrogen bond net, the conformations of Aβ converted from β-sheet non-β-sheet conformations, which destabilized the aggregation of Aβ into fibrils.