In-Silico Virtual Screening of Novel Antitoxic Agents from Talinum paniculatum as Inhibitors of Phospholipase A2 and Metalloproteinase Receptor for Antivenom Study

Health agencies have reported deaths from the envenomation of snakes, scorpions, and spiders to be a global challenge. Phospholipase A2 (PLA2) and metalloproteinase have been investigated to be major venom enzymes and their inhibition is important for antivenom experimentation. Varespladib (and other drugs such as varespladib-methyl and darapladib) has been mostly used as an antivenin but its cytotoxicity and the drive to source for effective drugs from phytomedicine with little or no side effects and higher potency led to the screening of bioactive compounds of Talinum paniculatum. The bioactive components of the plant with high binding affinities to the protein targets used were identified and subjected to further analysis and studies. After the molecular screening of the compounds of Talinum paniculatum ; rutin, kaempferol, quercetin, and Talinumoside1 were established to have high binding affinities to PLA2 and metalloproteinase in comparison to Varespladib (and other compounds such as varespladib-methyl, darapladib, marimastat and ilomastat) used for the study. Quercetin and kaempferol showed better results after the ADMET study and are better drug candidates than the other compounds studied. This research indicates that quercetin and kaempferol may inhibit PLA2, metalloproteinase, and potential antivenins. Further analysis is recommended to substantiate this study.