Conference Abstract | Volume 8, Abstract ELIC2025224 (Poster 041) | Published: 31 Jul 2025
Ayinde Abdulwahab Adeniyi1,2,&
1Faculty of Pharmaceutical Sciences, Bayero University, Kano, Nigeria, 2Chemoinformatics Academy
&Corresponding author: Ayinde Abdulwahab Adeniyi. Faculty of Pharmaceutical Sciences, Bayero University, Kano, Nigeria, Email: adeniyiabdulwahab3@gmail.com
Received: 24 Apr 2025, Accepted: 09 Jul 2025, Published: 31 Jul 2025
Domain: Infectious Disease Epidemiology
Keywords: Drug repurposing, anti-malaria drugs, dengue virus, molecular docking
©Ayinde Abdulwahab Adeniyi et al. Journal of Interventional Epidemiology and Public Health (ISSN: 2664-2824). This is an Open Access article distributed under the terms of the Creative Commons Attribution International 4.0 License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Cite this article: Ayinde Abdulwahab Adeniyi et al., Structure-based repurposing of anti-malaria drugs to inhibit RNA-dependent RNA polymerase domain of dengue virus. Journal of Interventional Epidemiology and Public Health. 2025;8(ConfProc5):00185. https://doi.org/10.37432/jieph-confpro5-00185
Dengue virus (DENV) is one of the most rapidly spreading mosquito-borne diseases worldwide, causing 100–400 million infections annually, with 96 million of those infections showing signs of severe illness. The RNA-dependent RNA polymerase (RdRp) catalytic domain resides within the NS5 protein from dengue virus and plays a vital role in the production of new viral particles. The aim of this study is to employ a structure-based approach for repurposing anti-malaria drugs to inhibit the RdRp domain of DENV.
A literature review of approved anti-malaria drugs was performed, and thirty-one (31) drugs were retrieved and downloaded from PubChem in SDF format. The crystal structure of the target receptor (2J7W) was obtained from the Protein Data Bank. The root mean square deviation (RMSD) was computed. The molecular docking and Molecular Mechanics/Generalized Born Surface Area (MM/GBSA) evaluation were performed using the Maestro Schrodinger software user interface. The physicochemical prediction and pharmacokinetic parameters for the top-ranking drugs were assessed using SwissADME web server.
The RMSD superposition for the minimized and redocked ligand was 1.4 Å. The docking scores (kcal/mol)/ MMGBSA (dG Bind) for the top five antimalarial drugs and the co crystalized ligand were tetracycline (6.494)/ (36.69), artesunate (4.4)/(35.17), chloroquine (4.109)/(40.66), chlorproguanil (4.021)/(34.18), 3 hydroxyquinine (4.01)/ (36.95), and co crystalized ligand (6.191)/(12.02) respectively. The physicochemical and pharmacokinetic properties of the drugs were found to be relatively good.
We identified highly potent inhibitors of dengue virus RdRp from the approved and currently available antimalarial drugs including chloroquine, 3-hydroxyquinine, tetracycline, artesunate, and chlorproguanil. However, in vitro and in vivo studies are required to provide more concrete information on the efficacy of these drugs.
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