Research Article
Docking Applied to the Study of Inhibitors of c-Met Kinase
Table 1
Biological data and docking results for quinoxaline derivatives.
| | Compound | c-Met IC50
(μM) | pIC50 | (Å) | Binding energy
(Kcal/mol) | Compound | c-Met IC50
(μM) | pIC50 | (Å) | Binding energy
(Kcal/mol) |
| | 1 | 1.3 | 5.886 | 1.80 | −11.6 | 18 | 0.8 | 6.097 | 1.93 | −11.9 | | 2 | | <4 | 1.92 | −10.5 | 19 | 12.9 | 4.889 | 2.24 | −10.5 | | 3 | 20.1 | 4.697 | 1.85 | −10.5 | 20 | 2.0 | 5.699 | 2.08 | −11.5 | | 4 | 5.3 | 5.276 | 1.78 | −11.3 | 21 | 0.39 | 6.409 | 2.09 | −12.0 | | 5 | | <4 | 2.18 | −10.5 | 22 | 0.17 | 6.770 | 1.94 | −12.0 | | 6 | 1.3 | 5.886 | 1.86 | −11.7 | 23 | 0.33 | 6.481 | 1.92 | −12.2 | | 7 | 19.6 | 4.708 | 2.34 | −10.7 | 24 | 1.9 | 5.721 | 1.94 | −11.7 | | 8 | 28.3 | 4.548 | 2.03 | −10.6 | 25 | 1.1 | 5.959 | 2.07 | −11.7 | | 9 | 3.9 | 5.409 | 1.98 | −11.2 | 26 | 7.1 | 5.149 | 2.78 | −11.4 | | 10 | 2.8 | 5.553 | 1.94 | −11.4 | 27 | 0.035 | 7.456 | 1.86 | −12.4 | | 11 | 5.0 | 5.301 | 1.86 | −11.4 | 28 | 0.54 | 6.268 | 2.02 | −11.9 | | 12 | 60.2 | 4.220 | 3.20 | −10.7 | 29 | 0.055 | 7.260 | 1.97 | −12.0 | | 13 | 1.5 | 5.824 | 2.19 | −11.2 | 30 | 0.32 | 6.495 | 2.03 | −11.8 | | 14 | 1.8 | 5.745 | 2.05 | −11.6 | 31 | 0.017 | 7.770 | 1.96 | −13.0 | | 15 | | <4 | 3.33 | −10.9 | 32 | 0.73 | 6.137 | 1.94 | −11.4 | | 16 | 5.0 | 5.301 | 3.35 | −11.1 | 33 | 0.031 | 7.509 | 2.02 | −12.4 | | 17 | 0.9 | 6.046 | 2.09 | −11.4 | 34 | 0.38 | 6.420 | 2.13 | −12.1 |
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aDistances derived from docking between the endocyclic N atom located at the positions 4 of the quinoxalines and the H atom of the MET1160.
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