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A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride

  • Rezaei Behbehani, G. (Chemistry Department, Imam Khomeini International University) ;
  • Divsalar, A. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Saboury, A.A. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Faridbod, F. (Departments of Chemistry, University of Tehran) ;
  • Ganjali, M.R. (Departments of Chemistry, University of Tehran)
  • Published : 2009.06.20

Abstract

Thermodynamics of the interaction between Cerium (III) chloride, $Ce^{3+}$, with Human Serum Albumin, HSA, was investigated at pH 7.0 and $27\;{^{\circ}C}$ in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by $Ce^{3+}$. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA with $Ce^{3+}$ showed a set of two binding sites with negative cooperativity. $Ce^{3+}$ interacts with multiple sites on HSA affecting its biochemical and biophysical properties.

Keywords

References

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