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Research Paper Open Access
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.
Leishmaniasis, trypanothione reductase, epicoccamide derivatives, in silico analysis