Envenomation resulting from snakebite is an important public health problem particularly in rural areas of Africa, Asia, and Latin America. Phospholipase A₂ and metalloprotease are some of the principal toxic components of snake venom. Hence, the inhibition of these enzymes is of pharmacological and therapeutic interest as they are involved in several hemorrhage and inflammatory diseases. This study employed in silico methods to provide insights into the inhibitory mechanism of 2',4'- dihydroxy-4-prenyloxychalcone and 3,5-dimethoxy-4'-O-(2,3-dihydroxy-3-methylbutyl)-dihydrostilbene isolated from the aerial parts of I. conferta on PLA₂ and metalloprotease snake venom. The method includes; predicting their ADME properties, molecular docking, molecular dynamics simulation, and binding free energy calculations. The result of the MD simulation revealed the average RMSD values for the C-α backbone atoms of PLA₂ in complex with the prenylated chalcone and the prenylated stilbene to be 1.14 and 1.16 Ǻ while that of metalloprotease in complex with prenylated chalcone and the prenylated stilbene were 1.37 and 1.18Å. Also, the electrostatic forces and van der Waals forces made a greater contribution to the total binding free energy in the PLA₂ complexes than in the metalloprotease complexes implying that the compounds exerted a greater inhibitory effect on the PLA₂ than on the Metalloprotease. The design of specific inhibitors of PLA₂ could help in the development of new pharmaceutical drugs, more specific antivenom, or even as alternative approaches for treating snakebites