Interaction and Binding Kinetics of Different Substituted Pyrazines with HSA: Based on Multispectral, Physiological Activity, and Molecular Dynamics Simulations

Table 2

Binding constants, number of binding sites, and thermodynamic parameters of 2,3-DMTP, 2,5-DMTP, TMTP, and TTMP interacting with HSA at different temperatures.

	T (K)	(L·mol^−1)	n	R	ΔH (kJ·mol^−1)	ΔG (L·mol^−1)	ΔS (L·mol^−1)
2,3-DMTP	291	1.4696 × 10^4	1.0852	0.9908	24.84	−23.26	165.04
	301	1.9888 × 10^4	1.1281	0.9987		−24.77
	310	2.7631 × 10^4	1.1609	0.9843		−26.36
2,5-DMTP	291	1.1956 × 10^4	1.0884	0.9705	17.62	−22.72	138.17
	301	1.2930 × 10^4	1.1056	0.9916		−23.70
	310	1.8858 × 10^4	1.1615	0.9968		−25.37
TMTP	291	1.4083 × 10^3	0.7909	0.9813	170.66	−17.54	644.16
	301	5.4731 × 10^3	0.9393	0.9991		−21.54
	310	1.1243 × 10^4	1.2600	0.9915		−29.98
TTMP	291	3.6091 × 10^4	1.0632	0.9990	15.17	−25.39	139.50
	301	4.6655 × 10^4	1.0968	0.9991		−26.90
	310	5.2856 × 10^4	1.1145	0.9989		−28.03