Study on the interaction of paeoniflorin with human serum albumin (HSA) by spectroscopic and molecular docking techniques

Table 1 Quenching constants (K_SV and K_q), stability constants (K_a), correlation coefficients (R) and binding site numbers (n) and thermodynamic parameters calculated according to Stern–Volmer plots and double logarithm plots of HSA + paeoniflorin system at three temperatures

HSA + paeoniflorin (K)	K_SV (L mol⁻¹)	K_q (L mol⁻¹ s⁻¹)	R²	K_A (L mol⁻¹)	n	∆G⁰ (kJ mol⁻¹)	∆H⁰ (kJ mol⁻¹)	∆S⁰ (J mol⁻¹ K⁻¹)
288	0.569 × 10⁴	0.9483 × 10¹²	0.9965	1.909 × 10³	0.9053	− 18.10
298	0.545 × 10⁴	0.9083 × 10¹²	0.9941	1.680 × 10³	0.8977	− 18.38	− 9.98	28.18
310	0.521 × 10⁴	0.8683 × 10¹²	0.9873	1.421 × 10³	0.8868	− 18.72

From 0.00 × 10⁻⁵ to 1.25 × 10⁻⁵ mol L⁻¹ at 2.50 × 10⁻⁶ mol L⁻¹ intervals ([HSA] = 1.0 × 10⁻⁵ mol L⁻¹, T = 288, 298 and 310 K)