Molecular simulation of the interaction between novel type rhodanine derivative probe and bovine serum albumin

The interaction between 3-(4′-methylphenyl)-5-(4′-methyl-2′-sulfophenylazo) rhodanine (M4MRASP) and bovine serum albumin (BSA) was studied by using spectrofluorimetry. It was shown in fluorescence spectrums that the quenching mechanism of BSA by M4MRASP was a static quenching. Meanwhile, the binding constant and binding site numbers were calculated. The action distance (r = 8.03 nm) and energy transfer efficiency (E = 0.12) between donor (BSA) and acceptor (M4MRASP) were obtained according to the theory of Förster non-radiation energy transfer. The effect of M4MRASP on the conformation of BSA was further analyzed by using synchronous fluorescence spectrometry. A new model of the interaction between small organic molecule and biomacromolecule was established. The results offered a reference for the studies on the biological effects and action mechanism of small molecule with protein.