Abstract
Malaria is the one most important parasitic disease of humans, which affects approximately one hundred countries and threatens half of the world’s population. The Plasmodium aspartic protease called plasmepsins performs a vital role in providing nutrients to the malaria parasite, which make these proteins as an excellent drug target. In this study, we have carried out a comparative protein modeling, active site analysis and structural analysis of all ten plasmepsins from Plasmodium falciparum. In this report we have analyzed in-silico structure modeling and made efforts to characterize plasmepsins structure and further propose its functional information. The phylogenetic analysis and disulfide linkages indicate, plasmepsin I to IV and HAP have similar structure, function property. Whereas, plasmepsin IX to X and plasmepsin VI to VIII belong to a separate cluster. The integral membrane protein plasmepsin V has a functional characterization as compared to the others aspartic proteases from Plasmodium falciparum. The overall study summarizes the need of good model to understand the structure and function activity and to design potent small molecule inhibitors targeting all ten plasmepsins, specifically Plasmepsin V as important target.
Highlights
Malaria is a life-threatening disease caused by Plasmodium parasites transmitted to humans through the infected Anopheles mosquitoes, in the region of tropical and subtropical climate and is active during the dusk and dawn [1]
In P. falciparum 3D7, the plasmepsin I-IV, VIII and IX genes are located in chromosome 14 whereas the plasmepsins V, VI, VII and X are localized on chromosome 13, 3, 10 and 8 respectively [54]
The instability index of plasmepsin VI, IX and X was computed by the server to be above 40 which predicts that the protein may be unstable
Summary
Malaria is a life-threatening disease caused by Plasmodium parasites transmitted to humans through the infected Anopheles mosquitoes, in the region of tropical and subtropical climate and is active during the dusk and dawn [1]. The structure-based drug design of antimalarial compounds targeting P. falciparum and the plasmepsin inhibitors have received much attention due to their potential therapeutic use [24,25]. The three dimensional (3D) structure of plasmepsin V was performed based on the homology modeling in PHYRE2 Protein Fold Recognition Server [45].
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