Evidence map›Paper›PMID 39896884›Full record

ArticleIn silico pharmacology2025

Allosteric activation of AMPK ADaM's site by structural analogs of Epigallocatechin and Galegine: computational molecular modeling investigation.

Mohnad Abdalla, Abdeen Tunde Ogunlana, Modinat Wuraola Akinboade, Ridwan Olajire Muraina, Oyindamola Anthonia Adeosun, Onyekachi Juliet Okpasuo, Olamide Tosin Olaoba, Abdulaziz Alouffi, Aqel Albutti, Zeyad Kurdee and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in In silico pharmacology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
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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

13 authors.

Mohnad AbdallaPediatric Research Institute, Children's Hospital Affiliated to Shandong University, Jinan, 250022 Shandong China.
Abdeen Tunde OgunlanaInstitute for Advanced Medical Research and Training, College of Medicine, University of Ibadan, Ibadan, Oyo State Nigeria.
Modinat Wuraola AkinboadeComputational Biology and Drug Discovery Laboratory, Department of Biochemistry, Faculty of Basic Medical Sciences, Ladoke Akintola University of Technology, Ogbomoso, Oyo State Nigeria.
Ridwan Olajire MurainaComputational Biology and Drug Discovery Laboratory, Department of Biochemistry, Faculty of Basic Medical Sciences, Ladoke Akintola University of Technology, Ogbomoso, Oyo State Nigeria.
Oyindamola Anthonia AdeosunComputational Biology and Drug Discovery Laboratory, Department of Biochemistry, Faculty of Basic Medical Sciences, Ladoke Akintola University of Technology, Ogbomoso, Oyo State Nigeria.
Onyekachi Juliet OkpasuoDepartment of Molecular Microbiology and Immunology, School of Medicine, University of Missouri, Columbia, MO 65212 USA.
Olamide Tosin OlaobaDepartment of Surgery, School of Medicine, University of Missouri, Columbia, MO 65212 USA.
Abdulaziz AlouffiKing Abdulaziz City for Science and Technology, Riyadh, 12354 Saudi Arabia.
Aqel AlbuttiDepartment of Medical Biotechnology, College of Applied Medical Sciences, Qassim University, Buraydah, Saudi Arabia.
Zeyad KurdeeClinical Biochemistry Unit, Department of Pathology, College of Medicine, King Saud University, Riyadh, 11461 Saudi Arabia.
Nouf Omar AlAfaleqDepartment of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
Ajibola Hannah FatoberuCambridge University Hospital, Cambridge, UK.
Temitope Isaac AdelusComputational Biology and Drug Discovery Laboratory, Department of Biochemistry, Faculty of Basic Medical Sciences, Ladoke Akintola University of Technology, Ogbomoso, Oyo State Nigeria.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

5'-Adenosine Monophosphate Protein Kinase (AMPK) is a central protein involved in cellular energy homeostasis, turning on catabolic pathways when the energy level is depleted and inhibiting anabolic pathways utilizing ATP. AMPK is implicated in several diseases including but not limited to diabetes, cancer, and cardiovascular diseases. Regulation of AMPK is cogent for restoring cellular energy levels which mediates the pathways leading to these diseases. Allosteric activation of AMPK via a novel ADaM site is intended for study in this case. In the search for AMPK activators, this study engaged a database for a virtual screening campaign through the ZINC15 database involving pharmacophoric modeling of two reported natural bioactive AMPK activators- Galegine and Epigallocatechin. Generated pharmacophores were targeted against the AMPK-ADaM site by employing various tools within the structure-based drug discovery process among which include consensus molecular docking, physicochemical profiling, ADMET, and molecular dynamics simulation. Advanced methods such as molecular mechanics (MM/GBSA) and quantitative structure-activity relationship (QSAR) were also performed. This investigation revealed promising pharmacophores that show better interactions and pharmacokinetic properties compared to the standards. This study proposes further development of these pharmacophores into potential drugs with better efficacies that could enhance the activation of the AMPK-ADaM site in ameliorating the aforementioned diseases. Supplementary Information: The online version contains supplementary material available at 10.1007/s40203-025-00311-x.

Indexed as

AMPK-ADaM siteAnd MM/GBSAMolecular dynamics simulationMolecular modelingPharmacophoric analogsVirtual screening

Identifiers

PMID39896884
PMCPMC11782767

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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.