A Spectroscopic and Molecular Docking Study on the Interaction of 2ʹ-Hydroxyflavanone with Bovine Serum Albumin

Flavonoids have a broad area of anatomical interest and as such, it is vital to understand their association behaviour with proteins. Here, under biological conditions, the interaction of 2ʹ-hydroxyflavanone (2HF) with cattle protein (BSA) was investigated using steady-state UV-Visible and fluorescence spectroscopy, FT-Infra Red spectroscopy, circular dichroism, and docking investigations. Analysis showed static quenching of BSA in presence of 2HF. FRET analysis showed possibilities of energy transfer between 2HF and BSA. Experiments and molecular docking results indicate 2HF binds to subdomain IIA of BSA. The thermodynamic parameters like ∆H, ∆S, and ∆G indicate that the association with 2HF is spontaneous, exothermic, and involves van der Waals force and H-bonding. By using FTIR and CD investigations demonstrate structural changes in BSA following a drug interaction. The conformational and functionality change of serum albumin (BSA) after association with the drug is further depicted by esterase-like activity study of serum albumin in presence of 2HF. The binding of the BSA-2HF complex decreased in presence of selected metallic ions.