Distinct Binding Dynamics, Sites and Interactions of Fullerene and Fullerenols with Amyloid-β Peptides Revealed by Molecular Dynamics Simulations.

ABSTRACT: The pathology Alzheimer's disease (AD) is associated with the self-assembly of amyloid-β (Aβ) peptides into β-sheet enriched fibrillar aggregates. A promising treatment strategy is focused on the inhibition of amyloid fibrillization of Aβ peptide. Fullerene C₆₀ is proved to effectively inhibit Aβ fibrillation while the poor water-solubility restricts its use as a biomedicine agent. In this work, we examined the interaction of fullerene C₆₀ and water-soluble fullerenol C₆₀(OH)₆/C₆₀(OH)₁₂ (C₆₀ carrying 6/12 hydroxyl groups) with preformed Aβ_40/42 protofibrils by multiple molecular dynamics simulations. We found that when binding to the Aβ₄₂ protofibril, C₆₀, C₆₀(OH)_6<

SUBMITTER: Liu Z 

PROVIDER: S-EPMC6514889 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature