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Docking simulations were performed on series (Hetero)arlylidene-(4-substituted-thiazol-2-yl)hydrazines as MAO-B inhibitors. This was done by analyzing the interaction of these compounds with the catalytic site of the MAO-B enzyme. Assuming that the enzyme inhibition is a function of the interaction energy, from a comparison with pIC50 a good correlation between theoretical and experimental data was observed. This suggests that identified binding conformations of these inhibitors are reliable. The results of docking studies provide an insight into the pharmacophoric structural requirements for the MAO-B inhibitory activity of these class molecules.
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Author(s): Grewal GK Rawal RK