Abstract

G. Rezaei Behbehani

Binding parameters of the N-phenyl benzene sulfonyl hydrazide, sulfonamide, and nanosulfonamide interaction with Human serum albumin were determined by calorimetry method. The obtained binding parameters indicated that sulfonamide in the second binding sites has higher affinity for binding than the first binding sites. The binding process of sulfonamide to HSA is both enthalpy and entropy driven. The association equilibrium constants confirm that sufonamide binds to HSA with high affinity (2.2×10⁶ and 3.8610⁵ M^-1 for first and second set of binding sites, respectively). The obtained results indicate that sulfonamide increases the HSA ani-oxidant property. Nanosulfonamide has much more affinity for HSA (3.6×10⁶ M^-1)) than sulfonamide.

Isothermal Titration Calorimetry; Sulfonamide; Nanosulfonamide; Human serum albumin; Binding sites

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