Molecular modelling and in silico analysis of p-methoxy cinnamoyl hydrazide analogues as Checkpoint Kinase-1 and aromatase inhibitors

The development of anticancer drugs from ethyl p-methoxycinnamate (epmc) derivatives has been done to compounds high activity in inducing cancer cells apoptosis and minimal side effects. p-methoxycinnamoyl hydrazide derivates, modified from epmc structure, were docked into the ligand-binding pocket of check point kinase 1 enzymes (2ywp) and the aromatase enzyme (3s7s) using software molegro virtual docker (mvd) ver.5.5. we compared the rerank score of native ligand with p-methoxycinnamoyl hydrazide derivates. rerank scores of compounds 4b and 4c (-99.98 kcal/mol and -99.80 kcal/mol) were lower than the native ligand a42 in inhibiting the enzyme checkpoint kinase 1. rerank values of p-methoxycinnamoyl hydrazide derivate compounds were greater than the native ligand exm in inhibiting the enzyme aromatase. p-methoxycinnamoyl hydrazide derivate compounds, especially compounds 4b and 4c, had anticancer mechanism by inhibiting the checkpoint kinase 1 enzyme pathway and showed no activity in inhibiting the aromatase enzyme.