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Aggregation of amyloid-β (Aβ) peptides is a crucial step in the progression of Alzheimer's disease (AD). Identifying aggregation inhibitors against AD has been a great challenge. We report an atomistic… Click to show full abstract
Aggregation of amyloid-β (Aβ) peptides is a crucial step in the progression of Alzheimer's disease (AD). Identifying aggregation inhibitors against AD has been a great challenge. We report an atomistic simulation study of the inhibition mechanism of two small molecules, homotaurine and scyllo-inositol, which are AD drug candidates currently under investigation. We show that both small molecules promote a conformational change of Aβ42 monomer toward a more collapsed phase through a non-specific binding mechanism. This finding provides atomistic-level insights into designing potential drug candidates for future AD treatments.
Journal Title: Journal of chemical theory and computation
Year Published: 2019
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