Glutathione S Transferase catalyse the conjugation of glutathione with a wide mixed bag of hydrophobic mixes, for the most part bringing about nontoxic items that could be readily killed. As opposed to different organisms, the malarial parasite Plasmodium falciparum has one Glutathione S Transferase enzyme (Pfgst). This Glutathione S Transferase is highly found in the parasite, its movement was discovered to be increased in chloroquine cells, and it has been indicated to go about as a ligand in for parasitotoxic hemin. Thus, the enzyme speaks to a guaranteeing target for antimalarial drug development. The target is docked with small ligand molecules with AutoDock Vina. The ligand molecules are checked for their toxicity Pfgst has a shorter C-terminal area bringing about a more dissolvable-available binding site for the hydrophobic substrates. The ligand molecules selected for docking are used for the inhibition of the Glutathione S Transferase molecule. The ligands that are selected are chloroquine, S hexylglutathione, Artemesinin, Hemin, Protoporphyrin IX, Tetracycline, Quinidine and Quinine. The ligand molecules are found to inhibit the Glutathione S Transferase molecule in vivo. These findings thus suggest that above molecules can may be potentially used for the drug development of malaria
