In Silico Approach Triterpene Glycoside of H. atra Targeting Orotidine 5-Monophosphate Decarboxylase Protein (PfOMPDC) in P. falciparum Infection Mechanism

This study accessed the potential antimalarial activity of triterpene glycoside of H. atra through targeting orotidine 5-monophosphate decarboxylase protein (PfOMPDC) in P. falciparum by molecular docking. Nine triterpene glycosides from H. atra extract modeled the structure by the Corina web server...

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Published in:BioMed research international 2024, Vol.2024, p.5924799-14
Main Authors: Utami, Prawesty Diah, Setianingsih, Herin, Sari, Dewi Ratih Tirto
Format: Article
Language:English
Subjects:
Antimalarial activity
Antiparasitic agents
Binding energy
Drug development
Fourier transforms
Glycosides
Hydrogen bonding
Hydrogen bonds
Hydrophobicity
In vivo methods and tests
Infections
Malaria
Molecular docking
Morbidity
Mortality
Parasites
Pharmacokinetics
Pharmacology
Proteins
Residues
Thermodynamics
Toxicity
Vector-borne diseases
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description This study accessed the potential antimalarial activity of triterpene glycoside of H. atra through targeting orotidine 5-monophosphate decarboxylase protein (PfOMPDC) in P. falciparum by molecular docking. Nine triterpene glycosides from H. atra extract modeled the structure by the Corina web server and interacted with PfOMPDC protein by using Hex 8.0.0. The docking results were visualized and analyzed by Discovery Studio version 21.1.1. 17-Hydroxyfuscocineroside B showed the lowest binding energy in PfOMPDC interaction, which was -1,098.13 kJ/mol. Holothurin A3, echinoside A, and fuscocineroside C showed low binding energy. Nine triterpene glycosides of H. atra performed interaction with PfOMPDC protein at the same region. Holothurin A1 posed interaction with PfOMPDC protein by 8 hydrogen bonds, 3 hydrophobic interactions, and 8 unfavorable bonds. Several residues were detected in the same active sites of other triterpene glycosides. Residue TYR111 was identified in all triterpene glycoside complexes, except holothurin A3 and calcigeroside B. In summary, the triterpene glycoside of H. atra is potentially a drug candidate for malaria therapeutic agents. In vitro and in vivo studies were required for further investigation.
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Nine triterpene glycosides from H. atra extract modeled the structure by the Corina web server and interacted with PfOMPDC protein by using Hex 8.0.0. The docking results were visualized and analyzed by Discovery Studio version 21.1.1. 17-Hydroxyfuscocineroside B showed the lowest binding energy in PfOMPDC interaction, which was -1,098.13 kJ/mol. Holothurin A3, echinoside A, and fuscocineroside C showed low binding energy. Nine triterpene glycosides of H. atra performed interaction with PfOMPDC protein at the same region. Holothurin A1 posed interaction with PfOMPDC protein by 8 hydrogen bonds, 3 hydrophobic interactions, and 8 unfavorable bonds. Several residues were detected in the same active sites of other triterpene glycosides. Residue TYR111 was identified in all triterpene glycoside complexes, except holothurin A3 and calcigeroside B. In summary, the triterpene glycoside of H. atra is potentially a drug candidate for malaria therapeutic agents. In vitro and in vivo studies were required for further investigation.</abstract><cop>United States</cop><pub>Hindawi</pub><pmid>38590385</pmid><doi>10.1155/2024/5924799</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0002-8527-4953</orcidid><oa>free_for_read</oa></addata></record>
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subjects Antimalarial activity
Antiparasitic agents
Binding energy
Drug development
Fourier transforms
Glycosides
Hydrogen bonding
Hydrogen bonds
Hydrophobicity
In vivo methods and tests
Infections
Malaria
Molecular docking
Morbidity
Mortality
Parasites
Pharmacokinetics
Pharmacology
Proteins
Residues
Thermodynamics
Toxicity
Vector-borne diseases
title In Silico Approach Triterpene Glycoside of H. atra Targeting Orotidine 5-Monophosphate Decarboxylase Protein (PfOMPDC) in P. falciparum Infection Mechanism
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