Computational view of beta-asarone-human serum albumin interaction
Document Type
Article
Publication Date
8-15-2022
Abstract
β-Asarone (BAS), a bioactive phytochemical from the medicinal herb, Acorus calamus Linn., has shown many pharmacological activities. Computational docking studies unveiled the interaction site of BAS onthe human plasma carrier, albumin. The primary binding arrangement of BAS was placed at Sudlow's Site I of HSA, which is pinpointed in subdomain IIA of albumin. Hydrophobic and van der Waals forces together with hydrogen bonds appear to secure the BAS-albumin complex. The BAS at Site I was surrounded by more hydrophobic and polar residues than those seen at Site II, as evidenced by LigPlot+. Therefore, the interaction between BAS and albumin at Site I seems to be comparatively more stable owing to more vital interactions. © 2021 by the authors.
Keywords
β-asarone, Human serum albumin, Drug-albumin interaction, Computational docking, Cluster analysis
Divisions
Science
Funders
Universiti Malaya Frontier Research Grant (FRG) [Grant No: FG025-17AFR]
Publication Title
Biointerface Research in Applied Chemistry
Volume
12
Issue
4
Publisher
AMG Transcend Association