Abstract:

The interaction of diacerein with human serum albumin(HSA) in physiological solution was studied by fluorescence spectroscopy. The result shows that diacerein quenches the fluorescence of HSA in a static quenching mode. The binding equilibrium constant KA and numbers of binding site n at different temperatures were calculated using two methods, which were compared in the work. The thermodynamic parameters obtained from measured data showed that the binding of diacerein to HSA involved hydrogen bonding and van der Waals interactions. According to the theory of energy transfer, the binding distance(r=2,88 nm) and transfer efficiency of energy(E=0,273 8) between diacerein and HSA were determined. The effect of diacerein on the conformation of HSA was also analyzed by synchronous fluorescence spectrometry.

Key words: diacerein, human serum albumin, fluorescence spectroscopy, interaction