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.

Quenching of fluorescence by meclizine, a probe study for structural and conformational changes in human serum albumin.

The goal of this study was to investigate the interactions between meclizine (MEC) and human serum albumin (HSA) under physiological conditions by different spectroscopies and molecular modeling technique. The drug, MEC quenched the intrinsic fluorescence of HSA and the analysis of the results revealed that static quenching mechanism. The binding of MEC quenches the HSA fluorescence; stoichiometry was 1:1 interaction.

Study of fluorescence interaction and conformational changes of bovine serum albumin with histamine H₁ -receptor--drug epinastine hydrochloride by spectroscopic and time-resolved fluorescence methods.

The fluorescence, ultraviolet (UV) absorption, time resolved techniques, circular dichroism (CD), and infrared spectral methods were explored as tools to investigate the interaction between histamine H1 drug, epinastine hydrochloride (EPN), and bovine serum albumin (BSA) under simulated physiological conditions. The experimental results showed that the quenching of the BSA by EPN was static quenching mechanism and also confirmed by lifetime measurements. The value of n close to unity indicated that one molecule of EPN was bound to protein molecule.