The mechanism of the interaction between curcumin and bovine serum albumin using fluorescence spectrum

The interaction between curcumin (CUR) and bovine serum albumin (BSA) in physiological buffer (pH 7.4) was investigated by fluorescence and UV-vis absorption spectroscopy at 298, 306 and 313 K. The results revealed that CUR could strongly quench the intrinsic fluorescence of BSA through a static quenching procedure. The binding constant K and number of binding sites n of CUR with BSA were measured by fluorescence quenching method. The thermodynamic parameters, enthalpy change (Delta H) and entropy change (Delta S), were calculated to be-64.11 kJ mol(-1) < 0 and-95.53 J mol-1 K-1 < 0, which respectively indicated that the interaction of CUR with BSA was driven mainly by the van der Waals force or hydrogen bond formation. The UV and AFM results found that the CUR and BSA could interact to form complex structures.