Characterization of interaction between bergenin and human serum albumin in membrane mimetic environments.

The interaction between bergenin and human serum albumin (HSA) in AOT/isooctane/water microemulsions was studied by fluorescence quenching technique in combination with UV absorption spectroscopy, circular dichroism (CD) spectroscopy and dynamic light scattering (DLS) technique. Fluorescence data in omega (o) 20 microemulsions revealed the presence of a binding site of bergenin on HSA and its binding constants (K) were 1.64 x 10(4), 1.44 x 10(4), 1.26 x 10(4) and 1.09 x 10(4) M(-1) at 289, 296, 303, and 310 K, respectively. The binding of bergenin with HSA in microemulsions was stronger than that in buffer solution. The alterations of protein secondary structure in the microemulsions in the absence and presence of bergenin compared with the free form of HSA in buffer were qualitatively and quantitatively analyzed by the evidence from CD spectra. Enthalpy and entropy changes for the reaction were calculated to be -14.45 kJ mol(-1) and 30.76 J mol(-1) K(-1). These results indicated that bergenin bound to HSA mainly by a hydrophobic interaction in microemulsions which was in agreement with the result of the molecular modeling study. The DLS data suggested that HSA may locate at the interface of the microemulsion and bergenin could interact with them.