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The interaction of both ferric (Fe³⁺) and cupric (Cu²⁺) ions with human serum albumin (HSA) was assayed at a temperature of 27°C in aqueous solution using isothermal titration calorimetry. The association equilibrium constant and the molar enthalpy for one binding is 1.7 × 10⁵ M-1 and -31.37 kJ • M⁻¹, respectively. To obtain the binding parameters of metal ion-protein interaction over the whole range of Fe³⁺ concentrations, the extended solvation model was applied. The solvation parameters obtained from this model were attributed to the structural change of HSA. The binding parameters obtained from the extended solvation model indicate that the stability of HSA was decreased as a result of its binding with ferric ions, which cause dampening the antioxidant property of HSA. Cuperic ion increases the stability of HSA considerably, indicating that the antioxidant property of human serum albumin are increased as a result of its interaction with cupric ion.

The effect of cupric and ferric ions on antioxidant properties of human serum albumin