Evidence map›Paper›PMID 41739386›Full record

ArticleMolecular diversity2026

Integrative computational and experimental identification of marine bacterial acetylcholinesterase inhibitors against alzheimer's disease.

Mohammed H Alqarni, Talha Jawaid, Saif Ahmed, Aftab Alam

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular diversity, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
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

4 authors.

Mohammed H AlqarniDepartment of Pharmacognosy, College of Pharmacy, Prince Sattam Bin Abdulaziz University, Al Kharj, 11942, Saudi Arabia.
Talha JawaidDepartment of Pharmacology, College of Medicine, Imam Mohammad Ibn Saud Islamic University (IMSIU), Riyadh, 13317, Saudi Arabia.
Saif AhmedDepartment of Anatomy & Physiology, College of Medicine, Imam Mohammad Ibn Saud Islamic University (IMSIU), Riyadh, 13317, Saudi Arabia.
Aftab AlamDepartment of Pharmacognosy, College of Pharmacy, Prince Sattam Bin Abdulaziz University, Al Kharj, 11942, Saudi Arabia. a.alam@psau.edu.sa.

Funding

Prince Sattam bin Abdulaziz University PSAU/2025/03/33451
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a powerful neurodegenerative disease characterized by cholinergic deficiency, where the inhibition of acetylcholinesterase (AChE) remains a clinically validated strategy. In our current work, a virtual screening platform supported by machine learning identified new inhibitors of AChE out of a structurally diverse collection of 2,895 marine bacterial natural products. Following a curation based on a structure-based strategy, a robust regression model was constructed from the physicochemical and structural characteristics of the reported inhibitors of AChE in an attempt to predict the inhibitory strength (pIC₅₀) of the top-scored ligands. The model had high predictive fidelity and led to the selection of twenty prospective candidates, out of which three (CMNPD25858, CMNPD28646, and CMNPD28412) were shortlisted according to activity profiles and drug-likeness filters. The shortlisted compounds were prepared for quantum-level refinement through density functional theory in order to improve electronic and structural precision. These optimised ligands were then evaluated under physiological conditions in terms of binding stability, conformational study, and intermolecular interaction through all-atom molecular dynamics simulation. CMNPD25858 demonstrated outstanding structural retention, stable persistent hydrogen bonding, and negligible displacement in the catalytic site. Principal component analysis and free energy landscape mapping revealed a highly confined, energetically favorable conformational basin. Structural overlays of post-simulation minima with initial docking poses confirmed minimal divergence. MM-GBSA free energy calculations substantiated the superior binding affinities of CMNPD25858 (-87.90 kcal/mol) and CMNPD28646 (-83.44 kcal/mol) relative to the reference compound. In vitro AChE inhibition assays revealed that compound CMNPD25858 demonstrated the highest inhibition (75%) at 1 mg/ml, followed by CMNPD28646 (64%) and CMNPD28412 (57.81%), consistent with in silico predictions when compared to the standard Donepezil (95.27%). Therefore, these integrative studies highlight the strategic utility of machine learning in accelerating structure-activity prediction and rational hit selection, and identifies marine-derived CMNPD25858 and CMNPD28646 as potent, dynamically stable AChE inhibitors with high potential for anti-Alzheimer's therapeutic development.

Indexed as

AcetylcholinesteraseAlzheimer DiseaseAquatic OrganismsBacteriaCholinesterase InhibitorsHumansLigandsMolecular Docking SimulationMolecular Dynamics SimulationStructure-Activity RelationshipAcetylcholinesteraseCholinesterase InhibitorsLigandsAcetylcholinesteraseAlzheimer’s diseaseMachine learningMarine bacteriaNeurodegenerative disease

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.