Exploring the binding interactions of bicalutamide with bovine serum albumin: spectroscopic techniques and molecular modeling studies.

The current study employed a variety of spectroscopic methods and molecular modeling to thoroughly look at, under physiological settings, the interaction between bicalutamide (BIC) and bovine serum albumin (BSA). According to our study, the BSA-BIC system's static quenching procedure is supported by the Stern-Volmer quenching constants. The binding constant dropped with temperature, implying that the BSA-BIC complex was weakened.

Binding of fexofenadine hydrochloride to bovine serum albumin: structural considerations by spectroscopic techniques and molecular docking.

The binding interaction of peripheral H receptor antagonist drug, fexofenadine hydrochloride to bovine serum albumin (BSA) is investigated by fluorescence spectroscopy in combination with UV-absorption spectroscopy under physiological conditions. The Stern-Volmer plots at different temperatures and the steady state fluorescence suggested a static type of interaction between fexofenadine and BSA. Binding constants were determined to provide a measure of the binding affinity between fexofenadine and BSA.

Evaluation of the binding interaction between bovine serum albumin and dimethyl fumarate, an anti-inflammatory drug by multispectroscopic methods.

The information of the quenching reaction of bovine serum albumin with dimethyl fumarate is obtained by multi-spectroscopic methods. The number of binding sites, n and binding constants, KA were determined at different temperatures. The effect of increasing temperature on Stern-Volmer quenching constants (KD) indicates that a dynamic quenching mechanism is involved in the interaction.