In silico study on evaluation of corosolic acid of Lagerstroemia speciosa against Alzheimer’s disease

Abstract

Purpose: Alzheimer’s disease (AD), the most common cause of dementia, is a neurodegenerative disorder caused by the aggregation of amyloid-beta (Aβ) at outside of neuron cells and also due to tau aggregation inside the cell. Corosolic acid is aimed to be selected as a main active constituent of Lagerstroemia speciosa for the study. Design/methodology/approach: In the present study, molecular docking of corosolic acid and tau protein was examined using PyRx-v.0.8 software. Absorption, Distribution, Metabolism, Excretion, and Toxicity (ADMET) properties were described and a molecular dynamics study of the bound complex was performed using Desmond. Findings: The docking score and interactions suggested that the corosolic acid (CID:6918774) could bind to tau protein to prevent the fibrillar network, to prevent AD. During simulation corosolic acid-bound protein root mean square deviation (RMSD) values showed more stability when compared to the Apo form of protein. Molecular dynamics study of tau protein and corosolic acid complex gave the insights to develop a drug-like candidate against AD. Originality/value: The use of corosolic acid of Lagerstroemia speciosa to prevent AD is supported by preliminary analysis on a computational basis. This compound should explore in terms of experimental strategies for the further drug development process. However, in vitro and in vivo evaluation studies are required to suggest the use of corosolic acid against AD.