Molecular dynamics simulation of Wrightiaionosides A from Wrightia Genus against wild-type and quadruple mutant pfDHFR.

Abstract

The dihydrofolate reductase domain of Plasmodium falciparum is a crucial target for anti-malarial drugs, but current treatments have been reduced due to the emergence of resistant parasites. A molecular dynamics simulation project was conducted to investigate the behavior of Wrightia genus compounds, specifically Wrightiaionoside A, when bound to the wild type and quadruple mutant of pfDHFR. The main objective was to identify potential new inhibitors using a molecular dynamic approach. The specific species, Wrightiaionoside A, was analyzed against both wild-type and quadruple mutant pfDHFR, and its fit into the active site was evaluated to determine its potential as an effective inhibitor.