Evidence map›Paper›PMID 40564438›Full record

ArticleBioengineering (Basel, Switzerland)2025

Discovery of Novel Natural Inhibitors of H5N1 Neuraminidase Using Integrated Molecular Modeling and ADMET Prediction.

Afaf Zekri, Mebarka Ouassaf, Shafi Ullah Khan, Kannan R R Rengasamy, Bader Y Alhatlani

Abstract read
In one paragraph

Article in Bioengineering (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

5 authors.

Afaf ZekriGroup of Computational and Medicinal Chemistry, LMCE Laboratory, University of Biskra, BP 145, Biskra 07000, Algeria.ORCID 0000-0001-5475-9707
Mebarka OuassafGroup of Computational and Medicinal Chemistry, LMCE Laboratory, University of Biskra, BP 145, Biskra 07000, Algeria.ORCID 0000-0002-0292-0949
Shafi Ullah KhanInserm U1086 ANTICIPE (Interdisciplinary Research Unit for Cancer Prevention and Treatment), Normandie University, Université de Caen Normandie, 14076 Caen, France.
Kannan R R RengasamyLaboratory of Natural Products and Medicinal Chemistry (LNPMC), Saveetha Medicinal College and Hospitals, Saveetha Institute of Medical and Technical Sciences (SIMATS), Thandalam, Chennai 602105, India.ORCID 0000-0001-7205-7389
Bader Y AlhatlaniUnit of Scientific Research, Applied College, Qassim University, Buraydah 52571, Saudi Arabia.ORCID 0000-0003-0871-6313

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The avian influenza virus, particularly the highly pathogenic H5N1 subtype, represents a significant public health threat due to its interspecies transmission potential and growing resistance to current antiviral therapies. To address this, the identification of novel and effective neuraminidase (NA) inhibitors is critical. In this study, an integrated in silico strategy was employed, beginning with the generation of an energy-optimized pharmacophore model (e-pharmacophore, ADDN) based on the reference inhibitor Zanamivir. A virtual screening of 47,781 natural compounds from the PubChem database was performed, followed by molecular docking validated through an enrichment assay. Promising hits were further evaluated via ADMET predictions, density functional theory (DFT) calculations to assess chemical reactivity, and molecular dynamics (MD) simulations to examine the stability of the ligand-protein complexes. Three lead compounds (C1: CID 102209473, C2: CID 85692821, and C3: CID 45379525) demonstrated strong binding affinity toward NA. Their ADMET profiles predicted favorable bioavailability and low toxicity. The DFT analyses indicated suitable chemical reactivity, particularly for C2 and C3. The MD simulations confirmed the structural stability of all three ligand-NA complexes, supported by robust and complementary intermolecular interactions. In contrast, Zanamivir exhibited limited hydrophobic interactions, compromising its binding stability within the active site. These findings offer a rational foundation for further experimental validation and the development of next-generation NA inhibitors derived from natural sources.

Indexed as

ADMETmolecular dockingmolecular dynamics simulationsneuraminidase inhibitorZanamivir

Identifiers

PMID40564438
PMCPMC12189692

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Registered trials

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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 OpenQuestion graph.