Thermodynamics of binding 2,2′-bipyridineglycinato palladium (II) chloride on human serum albumin

The interaction of human serum albumin (HSA) with 2,2'-bipyridineglycinato palladium (II) chloride was studied by isothermal titration microcalorimetry at 27 degrees C and equilibrium dialysis and UV-Vis. spectrophotometry techniques at temperatures of 27 & 37 degrees C in 2.5 mM phosphate buffer solution at pH = 7.0. The enthalpy of binding was calculated from binding data, which were obtained from equilibrium dialysis in terms of the Wyman binding potential theory related to the van't Hoff relation. The enthalpy of HSA unfolding was determined by subtraction of the microcalorimetric enthalpy (binding and unfolding enthalpies) and the enthalpy of binding. The enthalpy of HSA unfolding, due to the binding of that ligand, was 491.43 kJ mol(-1).