Plasmodium malariae is one of the causative agents of the deadly disease, malaria. From past few years, investigators have been vigorously involved in searching for an effective cure for this disease. However, the available drugs have not yet proven to be quite effi cient in its eradication primarily because of the advanced rate of mutation of the parasite. The present study is directed towards fi nding an inhibitor against plasmepsin II, one of the aspartic protease encoded by the malarial parasite, which is essential in degrading the host hemoglobin. The structure of the biological target was used to predict candidate drugs that could bind with high affi nity and selectivity to the target. The docking behaviour of target protein (2BJU) was studied in order to fi nd out the binding sites for the inhibitor on the protein molecule. The binding pocket that was selected had Phe84 and Thr341 as their active residues, depending upon which few ligand molecules were examined. Subsequently one of the ligand exhibited the best binding properties and the drug likeliness studies were carried out. Based on these studies, it could be inferred that the selected ligand could act as a potential drug candidate and thus, could also be considered for further studies.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.