Docking studies of Diphenylether Derivatives with Enoyl-ACP-Reductase of Plasmodium falciparum

Abstract

Malaria is one of the leading causes of death among infectious diseases. Among five species of the disease causing organisms, namely <i>Plasmodium<i>, two <i>P. falciparum<i> and <i>P. Vivax<i> are noxious. Diphenyl ethers are known to inhibit fatty acid biosynthesis in most organisms including <i>Plasmodium<i>. In this study, selected diphenyl ether molecules were docked against enoyl-Acyl Carrier Protein- reductase of <i>P. falciparum<i>. Using Triclosan, a known inhibitor of the enzyme, as standard fourteen molecules were docked using Autodock 4.0 and various interaction and binding energies were observed. Seven of the fourteen compounds were nitro while rest others were containing amino group at ortho position of the ether linkage. Compound 9 showed the least binding energy of -9.7 Kcal/mol as compared to -9.8 Kcal/mol for the standard triclosan. Compound 5 having nitro group displayed maximum binding energy -6.9 Kcal/mol and exhibits minimum affinity towards enoyl-Acyl Carrier Protein- reductase of <i>P. falciparum<i>.