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

Abstract

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. The BSA absorption spectra shifted to a lower wavelength area (from 278 to 272 nm) upon the addition of BIC. The distance (r) between the acceptor and donor in the complex of BIC-BSA and circular dichroism (CD) spectra show the molecular exchanges between BIC and BSA. This study is essential for understanding the therapeutic approach to cancer management through drug distribution and pharmacological effectiveness.