| Summary: | In this study, a set of 72 styryl lactone compounds reported from Goniothalamus species were docked against envelope (E), NS2B/NS3, NS5 methyltransferase (MTase), and NS5 RdRp dengue virus (DENV) protein. As a result, compounds 5, 37, 38, and 47 were identified as potential dengue protease inhibitors based on minimal docking energy values and multiple interactions with binding sites. The results from in-silico Lipinski's rule and ADMET analysis showed that these compounds were predicted to fulfil the drug-likeness properties. These ligands were found to fit in well and remain stable in the binding site of the envelope protein, NS2B/NS3, NS5 MTase, and NS5 RdRp. The results from molecular dynamic (MD) simulations indicate that the ligand-protein complex of compound 37 with NS5 MTase was stable throughout the MDs simulations and could interact with essential amino acids within the active sites. © 2022 World Scientific Publishing Company.
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