Open AccessStudy of Interaction Between Bovine Serum Albumin and Dolutegravir Intermediate: Fluorescence and Molecular Docking Analysis
Author(s) -
Susanta Kumar Behera,
Rubi Behura,
Patitapaban Mohanty,
Monalisha Sahoo,
Ramakrishna Duggirala Subrahmanya,
Anil Kumar Verma,
Bigyan Ranjan Jali
Publication year - 2021
Publication title -
biointerface research in applied chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.216
H-Index - 11
ISSN - 2069-5837
DOI - 10.33263/briac115.1310213110
Subject(s) - chemistry , docking (animal) , bovine serum albumin , fluorescence , titration , fluorescence spectroscopy , quenching (fluorescence) , binding site , fluorescence anisotropy , molecular model , stereochemistry , biochemistry , organic chemistry , medicine , physics , nursing , quantum mechanics , membrane
Novel (4R,12aS)-7-methoxy-4-methyl-6,8-dioxo-3,4,6,8,12,12a-hexahydro-2H-pyrido-[1',2':-4,5]-pyrazino[2,1-b][1,3]oxazine-9-carboxylic acid (L) was synthesized and characterised. The interaction between bovine serum albumin (BSA) with L was scrutinized by steady-state fluorescence spectroscopy, fluorescence anisotropy, fluorescence lifetime, and molecular docking methods. The fluorescence titration experiments of BSA resulted in fluorescence quenching with the incremental addition of L. The conformational binding of L to BSA has been investigated by molecular docking analysis. The molecular probe's best conformation showed the affinity as free binding energy release of -7.93 Kcal/mol. The docking analysis confirms that ligand binds in the near vicinity of TRP-213 in the binding pocket of subdomain IIA.