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. 527-535. ISSN 2394-0379

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Abstract

Aim:
Methodology:
Results:
Interpretation:
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 calculation
was carried out for the molecule lifted from the active site. Bader’s
theory of atoms in molecules (AIM) was used to determine the
electron 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.
A close observation of the results shows that diflunisal
has interactions in the binding sites IIA and IIIA of HSA as reported
earlier. Two strong classical H-bonding interactions, three
hydrophobic contacts with the amino acids VAL456, ALA194
andARG197, two close fluorine interactions, and two Pi-Sigma
interactions have been observed. Apart from the H-bond interactions, the stability of HAS-Diflunisal complex was further empathized by five
hyrdrophobic interactions framed between hydroxyl benzoic acid ring with ALA194, GLN459 and ARG197amino acid residue and difluorobenzene ring
with ALA194 and VAL456.
Theresults ofdrug-likeness study showedthatdiflunisal is highly reactiveandless toxic

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: 06 Oct 2022 05:27
Last Modified: 06 Oct 2022 05:27
URI: http://ir.psgcas.ac.in/id/eprint/1569

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