A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin

Table 1

Binding parameters for HAS + sulfonamide interaction. The interaction is both enthalpy and entropy driven, but the electrostatic interactions are more important than hydrophobic forces. 𝐾_𝑎 values show that sulfonamide in the second class of binding sites has higher affinity for binding than the first class of binding sites. The positive values of 𝛿^𝜃_𝐴 and 𝛿^𝜃_𝐵 indicate that the antioxidant property of HSA increased as a result of its interaction with sulfonamide.

Parameters	First binding sites	Second binding sites
𝑝	1	1
𝑔	1	4
𝐾𝑎/L·mol^−1	2.2×10^6±250	3.86×10^5±750
Δ𝐻/kJmol^−1	−24.63±0.08	−12.45±0.06
Δ𝐺/kJmol^−1	−30.57±0.08	−32.09±0.11
Δ𝑆/kJmol^−1K^−1	0.02±0.003	0.06±0.005
𝛿^𝜃𝐴	4.86
𝛿^𝜃𝐵		4.76