How Does the Mono-Triazole Derivative Modulate Aβ₄₂ Aggregation and Disrupt a Protofibril Structure: Insights from Molecular Dynamics Simulations.

ABSTRACT: Clinical studies have identified that abnormal self-assembly of amyloid-β (Aβ) peptide into toxic fibrillar aggregates is associated with the pathology of Alzheimer's disease (AD). The most acceptable therapeutic approach to stop the progression of AD is to inhibit the formation of β-sheet-rich structures. Recently, we designed and evaluated a series of novel mono-triazole derivatives 4(a-x), where compound 4v was identified as the most potent inhibitor of Aβ₄₂ aggregation and disaggregates preformed Aβ₄₂ fibrils significantly. Moreover, 4v strongly averts the Cu²⁺-induced Aβ₄₂ aggregation and disaggregates the preformed Cu²⁺-induced Aβ₄₂ fibrils, halts the generation of reactive oxygen species, a

SUBMITTER: Kaur A 

PROVIDER: S-EPMC7331201 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature