In this paper the interaction between tetramethyl-substituted BODIPY and bovine serum albumin (BSA) was studied using a spectroscopic approach (UV/vis spectrophotometry, spectrofluorimetry) and molecular docking. The fluorescence of tetramethyl-substituted BODIPY was found to substantially quenched in the presence of BSA. It was observed that BODIPY interacts with the BSA in the sub-domain site IIA of BSA. The BODIPY-BSA complex is formed due to the prevailing specific interactions.
