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. Author manuscript; available in PMC: 2021 Mar 26.
Published in final edited form as: J Med Chem. 2020 Mar 10;63(6):2854–2876. doi: 10.1021/acs.jmedchem.9b01189

Table 8.

Thermodynamic Binding Profiles of Selected Ligands with the Ligand Binding Domain of PPARα.a

graphic file with name nihms-1577324-t0030.jpg
Compound EC50 (μM) Kd (μM) ΔG
(kcal/mol)		 ΔH
(kcal/mol)		 −TΔS
(kcal/mol)
4a (A91) 4.43 ± 0.01 16.90 ± 1.50 −6.50 ± 0.05 −12.20 ± 1.40 5.71 ± 1.31
4b 0.77 ± 0.03 5.32 ± 0.78 −7.20 ± 0.09 −8.18 ± 0.20 0.98 ± 0.27
4u 0.037±0.005 0.14 ± 0.05 −9.39 ± 0.17 −7.75 ± 0.26 −1.65 ± 0.37
GW590735 0.015 ± 0.002 0.17 ± 0.03 −9.24 ± 0.09 −14.10 ± 0.50 4.90 ± 0.50
a

Buffer: 20 mM Hepes, 150 mM NaCl, pH 7.4. Ligand solution: 200–1000 μM ligand in buffer with 0.8–10% DMSO. Protein solution: 30–85 μM PPARα LBD in buffer with same concentration of DMSO as corresponding ligand solution. Thermodynamic parameters reported as mean ± S.D. of at least three separate experiments. All experiments were performed at 25 °C. N.D. = not determined.