Binding affinity studies of antipsychotic drugs with protein phosphatases by using auto dock vina

Protein Phosphatases play an important role in neuronal signaling pathway by dephosphorylating the phospho substrate which bring about a modulation either inhibitory or excitatory neuronal transmission. Antipsychotic drugs are used in the treatment of disorders like Schizophrenia, bipolar and psychosis. These drugs apparently act on receptors and regulate the neuronal signaling. However the mechanism of action is not very clear as one such antipsychotic drugs such as Trifluperazine (TFZ) acts on calmodulin and also inhibits the calcineurin (PP2B) activity. Hence in the current study we have tried to explore the binding affinities of three Antipsychotic drugs namely Olanzapine, Clozapine and trifluoparazine with six different Protein Phosphatases namely PP1, PP2A, PP2B, PP 2C, PP5 and PP7. These drugs were docked at their active sites of Protein Phosphatases using the Autodock Vina software (V4.0012). The binding energy (?G) scores for each of these drugs were determined. The TFZ exhibits highest binding affinity with PP2B compare to all other protein phosphatases. Atypical antipsychotic drugs Clozapine showed the lowest binding affinity with PP1, PP2A, PP2B and PP7. Whereas, Olanzapine showed the lowest binding affinity with PP2C and Trifluoparazine with PP5 suppose to be inhibitor of PP2B.Among all three drugs Clozapine showed the higher interaction with the protein phosphatases family PP1,PP2 and PP7. From this study we can conclude that all antipsychotic drugs do exhibit some degree of affinity towards different Protein phosphatases.