LAUSR

Abstract Through multispectroscopic and computational studies, interaction of drug Bisacodyl (BSL) with carrier proteins viz; Bovine Serum Albumin (BSA) and Human Serum Albumin (HSA) and Bovine Hemoglobin (BHb) have been studied. From this investigation, it has been found that BSL interacts with BSA, HSA and BHb via static quenching mechanism. The number of binding sites∼1 in all the complexes formed. The complexation resulted in conformational changes in the structure of proteins. Synchronous fluorescence study indicated that the quenching for Tryptophan residue was more than Tyrosine residue. UV spectroscopic study verified the complexation that occurred between BSA, HSA and BHb and BSL. CD spectra confirmed the conformation changes in the structure of BSA, HSA and BHb on successive addition of the drug. The observations of spectroscopic studies were in agreement with that of the computational study, showing complex formation.