Hybrid approach to sieve out natural compounds against dual targets in Alzheimer's Disease.

ABSTRACT: Excess Aβ production by the key protease BACE1, results in Aβ aggregation, forming amyloid plaques, all of which contribute to the pathogenesis of Alzheimer's disease. Besides the multi-factorial nature of the disease, the diversity in the size and shape of known ligands that bind to the active site of BACE1, that is the flexibility of the enzyme, pose a serious challenge for the identification of drug candidates. To address the issue of receptor flexibility we have carried out ensemble docking with multiple receptor conformations. Therein, two representative structures each from closed and semi-open BACE1 conformations were selected for virtual screening to identify compounds that bind to the active site of both the conformations. These outperformed compounds were ranked using pharmacopho

SUBMITTER: Das S 

PROVIDER: S-EPMC6403309 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature