Molecular docking study on the interaction between trypanothione reductase and mangiferin for antileishmanial activity

Abstract

Mangiferin was found to bind at active site of Leishmania infantum Try R with lowest binding energy and RMSD values to be -9.16 Kcal/Mol and 1.98 respectively. Docking analysis of Try R with ligand enabled us to identify specific residues viz. Phe-203, Glu-202, Asp-218, Pro-336, Try-221 and Phe-270, within the Try R binding pocket to play an important role in ligand binding affinity. The availability of Try R built model, together with insights gained from docking analysis will promote the rational design of potent and selective Try R inhibitor as antileishmanial therapeutic. The study contributes towards understanding mechanism of antileshmanial effect of the mangiferin. We have surveyed the available literature to summarize the inhibition of Try R activity of this natural compound. Thus on the basis of our in silico studies we hypothesize that this compound into mangiferin can be inhibitory effect on against leishmaniasis.