A new approach for thermodynamic study on the binding of human serum albumin with cerium chloride

Abstract

Thermodynamics of the interaction between Cerium (III) chloride, Ce3+, with Human Serum Albumin, HSA, was investigated at pH 7.0 and 27 °C in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by Ce3+. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA with Ce3+ showed a set of two binding sites with negative cooperativity. Ce3+ interacts with multiple sites on HSA affecting its biochemical and biophysical properties.