Abstract

G. Rezaei Behbehani and L. Barzegar

The thermodynamics interaction between new synthesized anti-cancer drugcomplex, Pd₂Py₂, and HSA wasinvestigated at pH 7 by isothermal titration calorimetry. The extended solvation model was used to reproduce the enthalpies of HSA interaction withPd₂Py₂. 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 Pd₂Py₂ and HSA indicated that the considerable conformational changes in HSA were not observed after binding toPd₂Py₂.

Human serum albumin; Anti-cancer; Isothermal titration calorimetry; Binding parameters

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