A Thermodynamic Study on the Binding of Human Serum Albumin with New synthesized Anticancer Pd(II) Complex

Abstract

The thermodynamics interaction between new synthesized anti-cancer drugcomplex, Pd 2 Py 2 , and HSA wasinvestigated at pH 7 by isothermal titration calorimetry. The extended solvation model was used to reproduce the enthalpies of HSA interaction withPd 2 Py 2 . The solvation parameters obtained from the new model was attributed to the structural change and anti-oxidant property of HSA. The binding parameters for the interaction of Pd 2 Py 2 and HSA indicated that the considerable conformational changes in HSA were not observed after binding toPd 2 Py 2 .