Interaction of Chrysophanol with Bovine Serum Albumin Using Spectroscopy and Molecular Modeling Techniques

The interaction of chrysophanol with bovine serum albumin(BSA) was investigated by fluorescence spectroscopy,synchronous fluorescence spectroscopy and molecular modeling techniques at different temperatures.The experimental results suggested that static quenching was the main reason for the fluorescence quenching process.Thermodynamic studies showed that the change for Gibbs free energy of the binding was a large negative value,which indicated that the interaction of chrysophanol with BSA was driven mainly by hydrophobic force.The results of molecular modeling indicated that there was not only hydrophobic interaction on the binding of chrysophanol to BSA,but there was also hydrogen bonding.The results of molecular modeling are in good agreement with those of spectral and thermodynamic studies.