A thermodynamic study on the binding of theophylline with human serum albumin

The thermodynamic parameters of interaction between theophylline and Human Serum Albumin (HSA) in buffer solution (30 mM) of pH = 7 at 27 °C was investigated by isothermal titration calorimetry (ITC). The thermodynamic quantities of the binding mechanism, the number of binding sites (g), the dissociation binding constant (Kd), the molar enthalpy of binding (ΔΗ) and other thermodynamic parameters can be obtained by the extended solvation theory.