Table 2.
ITC measurements for cholinesterase-ligand pairs. KD is the dissociation constant, n the binding stoichiometry, ΔH the binding heat, ΔG the Gibbs free energy of binding, and T∆S the entropy change, with ΔG = ΔH − T∆S. Where SDs are listed, the reported values are the mean ± SD of three independent experiments.
| Enzyme | Compound | KD (±SD) (µM) | n (±SD) | ΔH (±SD) (kJ·mol−1) | ΔG (±SD) (kJ·mol−1) | TΔS (kJ·mol−1) | ∆S (J·mol−1·K−1) |
|---|---|---|---|---|---|---|---|
| hAChE | Edrophonium | 1.4 ± 0.4 | 0.8 ± 0.3 | −26.4 ± 7.9 | −33.6 ± 0.8 | −7.2 | −24.2 |
| Ethopropazine | 26.7 ± 14.7 | 1.5 ± 0.3 | −10.9 ± 1.1 | −26.4 ± 1.6 | −15.5 | −52.0 | |
| Propidium | 6.7 ± 0.7 | 0.8 ± 0.1 | −45.4 ± 5.0 | −29.6 ± 0.3 | 15.8 | 52.9 | |
| Thioflavin-T | 17.7 | 1 | −23.7 | −27.2 | −3.5 | −11.8 | |
| hBChE | Edrophonium | 27.2 ± 2.4 | 0.9 ± 0.1 | −12.6 ± 1.7 | −26.1 ± 0.3 | −13.5 | −45.3 |
| Ethopropazine | 1.1 ± 0.1 | 1.0 ± 0.1 | −43.6 ± 6.4 | −34.1 ± 0.2 | 9.5 | 31.8 | |
| Propidium | 2.1 ± 0.4 | 0.8 ± 0.1 | −43.1 ± 19.1 | −31.7 ± 0.4 | 11.4 | 38.2 | |
| Thioflavin-T | 2.6 ± 0.5 | 2.2 ± 0.1 | −11.4 ± 0.6 | −32.0 ± 0.6 | −20.6 | −69.1 |