TIGP (BIO)—Uncovering Amyloid Beta Misfolding Mechanisms and Inhibitors: Insights from Molecular Docking and Dynamics Simulations

Abstract

Amyloid beta (Aβ) misfolding and aggregation are key pathological features of Alzheimer’s disease (AD), yet the molecular mechanisms underlying this process remain incompletely understood. In this study, we employ molecular docking and molecular dynamics (MD) simulations to investigate the structural dynamics, misfolding triggers, and potential inhibitors of Aβ aggregation. Our simulations reveal critical conformational changes and intermolecular interactions that promote fibril formation, identifying specific regions of Aβ prone to destabilization and aggregation. Furthermore, we evaluate a series of small-molecule compounds for their ability to stabilize native Aβ conformations and inhibit misfolding, highlighting key binding sites and inhibitory mechanisms. These findings provide valuable insights into the molecular basis of Aβ pathology and offer promising avenues for the development of novel AD therapeutics.

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