Scaffhold Hopping to Percept the Achiral Compound and Functionalizing on Target Protein Plasmepsin II

Abstract

Malaria is a vector-borne infectious disease caused by protozoan parasites of the genus Plasmodium. Four types of the plasmodium parasite can infect humans; the most serious forms of the diseases are caused by Plasmodium falciparum. Plasmepsin group of enzymes are key enzymes in the life cycle of malarial parasites. Plasmepsin II enzyme is responsible for the formation of the hemozoin through the hemoglobin degradation pathway. Specification of potential drug target by inhibiting Plasmepsin II Enzyme, N-(R-Carboxy-Ethyl)-Alpha-(S)-(2-Phenylethyl) presently used as an inhibitor, to prevent the degradation. Changeover of side chains based on isomeric property of Achiral compounds is aimed to be a new inhibitor for the Plasmepsin II enzyme. Scaffold hopping is an approach used to discover new chemical classes by replacing a portion (the scaffold) of a known compound, while preserving the remaining chemical groups, under the assumption that they are important for biological activity. The main goal of this investigation was to find out the types of combination with the ligand to be the most active in the inhibition of Plasmepsin II enzyme, among the Achiral compounds. Achiral inhibitors revealed exploitation of a new inhibitor observed in Plasmepsin II protein, by Electrostatic potential, binding energy, and bond interactions.