Version 1
: Received: 30 November 2023 / Approved: 1 December 2023 / Online: 1 December 2023 (04:07:30 CET)
How to cite:
Gupta, K.; Saggu, G. S. Isoprenoid Biosynthesis Pathway Enzymes As Promising Drug Candidates Against Malaria Parasites: An In-Silico Investigation. Preprints2023, 2023120032. https://doi.org/10.20944/preprints202312.0032.v1
Gupta, K.; Saggu, G. S. Isoprenoid Biosynthesis Pathway Enzymes As Promising Drug Candidates Against Malaria Parasites: An In-Silico Investigation. Preprints 2023, 2023120032. https://doi.org/10.20944/preprints202312.0032.v1
Gupta, K.; Saggu, G. S. Isoprenoid Biosynthesis Pathway Enzymes As Promising Drug Candidates Against Malaria Parasites: An In-Silico Investigation. Preprints2023, 2023120032. https://doi.org/10.20944/preprints202312.0032.v1
APA Style
Gupta, K., & Saggu, G. S. (2023). Isoprenoid Biosynthesis Pathway Enzymes As Promising Drug Candidates Against Malaria Parasites: An In-Silico Investigation. Preprints. https://doi.org/10.20944/preprints202312.0032.v1
Chicago/Turabian Style
Gupta, K. and Gagandeep Singh Saggu. 2023 "Isoprenoid Biosynthesis Pathway Enzymes As Promising Drug Candidates Against Malaria Parasites: An In-Silico Investigation" Preprints. https://doi.org/10.20944/preprints202312.0032.v1
Abstract
Malaria parasite harbors an essential prokaryotic-like organelle characterized by multiple mem-branes, akin to a plastid. This organelle, known as the apicoplast, evolved from secondary en-dosymbiosis. In this event, a photosynthetic alga was engulfed by a eukaryotic host and subsequently transformed into a symbiotic entity from its free-living origin. As a result, the apicoplast transformed into a remnant structure housing a circular genome, enveloped by four membranes. Concurrently, the host cell relinquished significant metabolic pathways, and a substantial portion of the apicoplast genome migrated to the host cell, establishing a symbiotic relationship. This unique symbiotic bond designates the apicoplast as a constrained environment for diverse metabolic pathways, vital for parasite survival. Notably, the non-mevalonate biosynthesis (MEP/DOXP) pathway is identified as pivotal for the parasite's viability across parasitic stages. In this study, we conducted a comparative analysis of Plasmodium falciparum MEP pathway enzymes, juxtaposing them with their counterparts in other apicomplexans, plants, and pathogenic microorganisms to uncover the conserved traits of these enzymes. Additionally, predictive modeling was employed to shed light on the protein structures, with specific emphasis on elucidating the active site characteristics and examining their binding affinities with various substrates and inhibitors. This article presents a comprehensive in-silico analysis of MEP pathway enzymes, showcasing their potential as prospective targets for innovative antimalarial drugs. The elucidation of these enzymes' intricate functions provides a foundation for the development of advanced therapeutic strategies in the battle against malaria.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
