In Silico Analyses of Epicoccamides on Selected Leishmania Trypanothione Reductase Enzyme-based Target
Department of Pharmacy, COMSATS Institute of Information Technology, Abbottabad 1Department of Chemistry, COMSATS Institute of Information Technology, Abbottabad 2University College of Pharmacy, University of Punjab, Lahore 3Institute of Molecular Biology and Biotechnology, Bahauddin Zakariya University, Multan, Pakistan
S. A. Muhammad Institute of Molecular Biology and Biotechnology, Bahauddin Zakariya University, Multan, Pakistan Email: [email protected]
Leishmaniasis is a protozoal infection which presents a broad spectrum drug resistance and causing diseases ranging from asymptomatic infections to significant mortality. The enzyme, trypanothione reductase from Leishmania infantumis is essential for the parasite survival. It is an attractive target to design new less toxic drugs against Leishmaniasis as found absent in mammalian cells. The antileishmanial activity of epicoccamide derivatives was studied by in silico approaches. The crystallographic structure of trypanothione reductase was obtained from the protein data bank (ID: 2W0H) database. Binding mode of the epicoccamide inhibitors showed that they are stabilized in the active site of enzyme through hydrogen bond and hydrophobic interactions. These derivatives (A-D) showed significant binding affinities with trypanothione reductase with binding energies: -13.21, -13.44, -13.31, and -13.52 kcal/mol, respectively.The present study showed new and effective antileishmanial compounds that can get pharmaceutical importance.