Spectral and molecular modelling studies of sulfadoxine interaction with bovine serum albumin

The present study is focused on the binding interaction of sulfadoxine with bovine serum albumin under simulated physiological conditions using spectrofluorimetry. Various spectroscopic and other methods like UV-vis, Raman, FTIR, CD, lifetime measurement, cyclic voltamrnetry were also employed during the course of study. It was noticeable that sulfadoxine did quench the intrinsic fluorescence of BSA via static quenching process. UV-vis study enabled the calculation of association constant, K-ass for the interaction of BSA and sulfadoxine. The change in the secondary structure of BSA and binding mechanism was investigated with the spectral and docking studies. The meticulous investigation of competitive binding sites using various probes was studied and it was clear that drug binding was non-specific. Effect of some co-existent drugs and metal ions were examined which may help in the controlled release of drugs.