David Stephen, A (2022) Evaluation of diflunisal a difluoro-derivative of salicylic acid as an inhibitor of human serum albumin using molecular docking tools. Journal of Environmental Biology, 43. pp. 1-9. ISSN 2394-0379

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Abstract

To evaluate the binding interaction of diflunisal at active site of Human Serum Albumin (HSA), an important enzyme responsible for osteoarthritis disease. The gas phase molecule was optimized with B3LYP/6-311G** basis set, while a single point energy calculationwas carried out for the molecule lifted from the active site. Bader’stheory of atoms in molecules (AIM) was used to determine theelectron density and Laplacian of electron density. The protein was assigned with polar hydrogens and Kollman charges. Iterated local
search procedure was performed during docking, during this, both protein and ligand were considered as rigid. Among the ten poses, lowest binding energy pose was considered for further ligand protein interaction analysis and QTAIM studies

Item Type: Article
Uncontrolled Keywords: Binding affinity, Diflunisal, Human Serum Albumin, Inflammation, Molecular docking, Pain
Divisions: PSG College of Arts and Science > Department of Physics
Depositing User: Mr Team Mosys
Date Deposited: 22 Jun 2022 03:48
Last Modified: 22 Jun 2022 03:48
URI: http://ir.psgcas.ac.in/id/eprint/1234

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