Molecular docking studies of bioactive compounds from the leaves of Epiphyllum oxypetalum against Treponema pallidum, Zika virus and liver cirrhosis

The Epiphyllum oxypetalum is a unique plant that belongs to a cactaceae family. Traditionally, this plant mainly curessexually transmitted diseases, liver infection, and antiviral disease. The molecular docking analysis was done againstvirulent bacterial and viral enzymes. The protein responsible for bacterial and viral disease were studied and retrievedfrom Protein Data Bank. The bioactive compounds of E. oxypetalum were docked against Treponema pallidum,liver cirrhosis, and Zika virus (ZIKV). The result obtained with better binding interactions against T. pallidum wasMegastigmatrienone with −5.02Kcal/mol followed by liver cirrhosis was Megastigmatrienone with −4.58Kcal/moland against ZIKV was Testerone cypionate with −7.84Kcal/mol. Thus, the molecular docking interactions showsbetter potential of inhibition against virulent enzymes and the bioactive compounds of E. oxypetalum leave whichcould be used as a lead for treating the diseases, such as Syphilis, liver cirrhosis, and ZIKV.

Molecular docking of various bioactive compounds from essential oil of Trachyaspermum ammi against the fungal enzyme Candidapepsin-1

The bioactive compounds from essential oil of Trachyaspermum ammi using gas chromatography–mass spectrometryand their inhibition potential against the enzyme Candidapepsin-1 were studied. The research work focuses on themolecular simulation of bioactive compounds against the enzyme that acts as a potential drug target and support thedrug discovery process. Candidapepsin-1 has been reported to be the cause for biofilm formation, superficial skininfections, and oral infections. Fifteen active compounds and their interactions with Candidapepsin-1 were studiedin this research work. The compounds satisfied Lipinski’s rule of five in order to be used as an oral drug. ADMETproperties of the compounds used to determine pharmacodynamic and pharmacokinetic properties which werereported in the study. The compounds were docked against the enzyme with the help of AutoDock 4.2.6 software.Ligustilide has the lowest free binding energy of −5.75 kcal/mol against the Candidapepsin-1 with three hydrogenbond interactions at Ile 223, Tyr 225, and Thr 222 at the active site of the enzyme followed by cedrane with −5.20kcal/mol. The hydrogen bond interactions, Vander Waals interactions, and two-dimensional and three-dimensionalinteractions were studied.