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. 2018 Apr 3;8:5497. doi: 10.1038/s41598-018-23920-3

Table 2.

Thermodynamic parameters of binding of apoA-I 1‒83/G26R to SUVs at 25 °Ca.

SUV Kd (μg/ml) Bmax (amino acids/mol PL) ΔGb (kcal/mol) ΔH (kcal/mol) TΔSc (kcal/mol)
PC 1.1 ± 0.5 0.14 ± 0.03 −11.9 ± 0.3 −20.3 ± 0.8 −8.4 ± 0.8
PC/Chol (2/1) 3.8 ± 0.4 0.12 ± 0.02 −11.1 ± 0.1 −24.6 ± 0.1 −13.5 ± 0.1
PC/PS (17/3) 1.0 ± 0.9 0.28 ± 0.07 −12.1 ± 0.6 −12.4 ± 0.1 −0.3 ± 0.6
PC/PS (7/3) 0.5 ± 0.4 0.53 ± 0.19 −11.6 ± 0.1 −11.6 ± 0.1 0.9 ± 0.5

aThe data were from three independent experiments.

bFree energy was calculated according to ΔG = −RT ln 55.5(1/Kd).

cThe entropy of binding was calculated from ΔG = ΔHTΔS.