Evidence mapPaperPMID 42511483Full record

ArticleInternational journal of molecular sciences2026

Ensemble Docking, MD, and MM/PBSA Identify Flavonoids as Putative Modulators of EFNB2/B3-Nipah Virus G Interaction.

Carlos Vargas-Echeverría, Oscar Saurith-Coronell, Olimpo Sierra-Hernandez, Juan F Santos-Rodríguez, Juan D Rodríguez-Macías, José R Mora, José L Paz, Breallan De Jesús Rómero Pájaro, German Darío Idarraga Negrete, Ricardo Olimpio de Moura and 2 more

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Carlos Vargas-EcheverríaDepartamento de Medicina, División Ciencias de la Salud, Universidad del Norte, Km 5, Vía Puerto Colombia, Puerto Colombia 081007, Colombia.ORCID 0009-0000-8160-3572
Oscar Saurith-CoronellDepartamento de Medicina, División Ciencias de la Salud, Universidad del Norte, Km 5, Vía Puerto Colombia, Puerto Colombia 081007, Colombia.ORCID 0009-0008-4454-3126
Olimpo Sierra-HernandezDepartamento de Medicina, División Ciencias de la Salud, Universidad del Norte, Km 5, Vía Puerto Colombia, Puerto Colombia 081007, Colombia.ORCID 0009-0004-8239-5890
Juan F Santos-RodríguezGrupo de Investigaciones en Química y Biología, Departamento de Química y Biología, Facultad de Ciencias Básicas, Universidad del Norte, Carrera 51B, Km 5, Vía Puerto Colombia, Barranquilla 081007, Colombia.ORCID 0009-0003-5673-6594
Juan D Rodríguez-MacíasFacultad de Ciencias de la Salud, Exactas y Naturales, Universidad Libre, Barranquilla 080001, Colombia.ORCID 0000-0001-5247-867X
José R MoraGrupo de Química Computacional y Teórica (QCT-USFQ), Departamento de Ingeniería Química, Universidad San Francisco de Quito, Diego de Robles y Vía Interoceánica, Quito 170901, Ecuador.ORCID 0000-0001-6128-9504
José L PazDepartamento Académico de Química Inorgánica, Facultad de Química e Ingeniería Química, Universidad Nacional Mayor de San Marcos, Lima 15081, Peru.ORCID 0000-0002-6177-7919
Breallan De Jesús Rómero PájaroEspecialización en Medicina Interna, Universidad Libre, Barranquilla 080001, Colombia.ORCID 0009-0003-2330-9166
German Darío Idarraga NegreteEspecialización en Medicina Interna, Universidad Libre, Barranquilla 080001, Colombia.
Ricardo Olimpio de MouraPrograma de Pós-Graduação em Ciências Farmacêuticas (PPGCF), Universidade Estadual da Paraíba (UEPB), Campina Grande 58429-500, PB, Brazil.ORCID 0000-0002-1590-3750
Igor José Dos Santos NascimentoPrograma de Pós-Graduação em Ciências Farmacêuticas (PPGCF), Universidade Estadual da Paraíba (UEPB), Campina Grande 58429-500, PB, Brazil.ORCID 0000-0002-2664-4336
Edgar A Márquez BrazónGrupo de Investigaciones en Química y Biología, Departamento de Química y Biología, Facultad de Ciencias Básicas, Universidad del Norte, Carrera 51B, Km 5, Vía Puerto Colombia, Barranquilla 081007, Colombia.ORCID 0000-0002-7503-1528

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nipah virus (NiV) is a highly lethal zoonotic pathogen with significant pandemic potential, for which no approved antiviral therapies are currently available. Viral entry is mediated by the interaction between the NiV attachment glycoprotein (NiV-G) and host ephrin receptors, particularly ephrin-B2 (EFNB2) and ephrin-B3 (EFNB3), making this interface an attractive therapeutic target. In this study, we evaluated a set of structurally related flavonoids, apigenin, cynaroside, and lonicerin, as potential modulators of the EFNB2-NiV-G and EFNB3-NiV-G interactions. These compounds were selected based on their structural similarity, reported antiviral activity, chemical diversity, and favorable drug-like properties. Apigenin was employed as a reference scaffold due to its well-characterized pharmacological profile and its suitability for guiding analog-based compound selection. Apigenin served as a reference scaffold for selecting structurally related flavonoids, which were analyzed through density functional theory optimization, molecular docking, pharmacokinetic and toxicity predictions, molecular dynamics simulations, and binding free energy calculations. These flavonoids demonstrated high predicted affinity for both the EFNB2-NiV-G and EFNB3-NiV-G interfaces. According to results, these compounds consistently interacted with residues known to play a critical role in receptor recognition, with special emphasis on leucine and tryptophan residues within the G-H loop. These residues are well established as key determinants in the entry process of Nipah virus (NiV) into host cells, highlighting the potential relevance of these flavonoid-protein interactions. Molecular dynamics analyses indicated that flavonoid binding reduced the affinity and the conformational flexibility at the receptor-glycoprotein interfaces and decreased the stability of the complexes. Pharmacokinetic and toxicity predictions suggested favorable drug-like properties for the flavonoids, with apigenin displaying the most balanced profile. Collectively, these results support the potential of selected flavonoids as modulators of EFNB2-NiV-G and EFNB3-NiV-G interactions and provide a rationale for their prioritization in experimental studies aimed at developing scaffolds for the modulation of viral entry against Nipah virus.

Indexed as

Ephrin-B2Ephrin-B3FlavonoidsMolecular Docking SimulationNipah VirusAntiviral AgentsHumansMolecular Dynamics SimulationProtein BindingVirus InternalizationAntiviral AgentsEphrin-B2Ephrin-B3Flavonoidsflavonoidsin silico scaffold discoverymolecular dynamics simulationsNipah virusviral entry modulation

Identifiers

PMID42511483
PMCPMC13410004

What Socratic holds

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.