Potential drug bis (2-ethylhexyl) phthalate target through docking analysis of the protein n-myristoryltransferase (pdb id: 4bbh) of plasmodium vivax

Malaria is a debilitating disease transmitted by mosquitoes and caused by protozoa of the genus Plasmodium. The disease is most commonly transmitted by an infected female Anopheles mosquito. The mosquito bite introduces the parasites from the mosquito's saliva into a person's blood. The parasites travel to the liver where they mature and reproduce. Chemical validation of new ant malarial targets is recently required in view of rising resistance to current drugs. The target receptor enzyme N-myristoyltransferase of Plasmodium vivax, which catalyzes N-myristoylation of protein substrates by the drug molecule, Bis (2ethylhexyl) phthalate. This work was aimed at the components obtained from the GC-MS analysis of Kalancho epinnata leaf extract and it act as lig and to bind with receptor protein molecules of malarial parasite. The docking simulation of compound is active on the active site of the Plasmodium vivax has been analysed. The result is suggested to found that phytochemical Bis (2 ethylhexyl) phthalate works more efficiently against the receptor protein of P. vivax. The screened inhibitors are effective and showed optimal binding affinity to the binding receptor of P.vivax. Its molecular properties and its binding affinity make it acceptable as a potential therapeutic against malaria.