Evidence map›Paper›PMID 38532068›Full record

ArticleScientific reports2024

A comprehensive computational study to explore promising natural bioactive compounds targeting glycosyltransferase MurG in Escherichia coli for potential drug development.

Amneh Shtaiwi, Shafi Ullah Khan, Meriem Khedraoui, Mohd Alaraj, Abdelouahid Samadi, Samir Chtita

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
7.8field-weighted citation impact, top 2% of its field
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

6 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Machine Learning-Enabled Drug-Induced Toxicity Prediction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  6. 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

6 authors at 5 institutions in 4 countries.

Amneh ShtaiwiFaculty of Pharmacy, Middle East University, Queen Alia Airport Street, Amman, P.O. Box No. 11610, Jordan. ashtaiwi@meu.edu.jo.ORCID 0000-0001-6081-7440
Shafi Ullah KhanInterdisciplinary Research Unit for Cancer Prevention and Treatment, Baclesse Cancer Centre, Université de Caen Normandie Inserm Anticipe UMR 1086, Normandie Univ, Research Building, F‑14000 François 3 Avenue Général Harris, BP 45026, 14076, Cedex 05 Caen, France.ORCID 0000-0001-9231-1831
Meriem KhedraouiLaboratory of Analytical and Molecular Chemistry, Faculty of Sciences Ben M'Sik, Hassan II University of Casablanca, B. P 7955, Casablanca, Morocco.
Mohd AlarajFaculty of Pharmacy, University of Jerash, Jerash, Jordan.
Abdelouahid SamadiDepartment of Chemistry, College of Science, UAEU, P.O. Box No. 15551, Al Ain, UAE. samadi@uaeu.ac.ae.
Samir ChtitaLaboratory of Analytical and Molecular Chemistry, Faculty of Sciences Ben M'Sik, Hassan II University of Casablanca, B. P 7955, Casablanca, Morocco.ORCID 0000-0003-2344-5101
University of Hassan II Casablanca · MAInserm · FRJerash University · JOMiddle East University · JOUnited Arab Emirates University · AE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptidoglycan is a carbohydrate with a cross-linked structure that protects the cytoplasmic membrane of bacterial cells from damage. The mechanism of peptidoglycan biosynthesis involves the main synthesizing enzyme glycosyltransferase MurG, which is known as a potential target for antibiotic therapy. Many MurG inhibitors have been recognized as MurG targets, but high toxicity and drug-resistant Escherichia coli strains remain the most important problems for further development. In addition, the discovery of selective MurG inhibitors has been limited to the synthesis of peptidoglycan-mimicking compounds. The present study employed drug discovery, such as virtual screening using molecular docking, drug likeness ADMET proprieties predictions, and molecular dynamics (MD) simulation, to identify potential natural products (NPs) for Escherichia coli. We conducted a screening of 30,926 NPs from the NPASS database. Subsequently, 20 of these compounds successfully passed the potency, pharmacokinetic, ADMET screening assays, and their validation was further confirmed through molecular docking. The best three hits and the standard were chosen for further MD simulations up to 400 ns and energy calculations to investigate the stability of the NPs-MurG complexes. The analyses of MD simulations and total binding energies suggested the higher stability of NPC272174. The potential compounds can be further explored in vivo and in vitro for promising novel antibacterial drug discovery.

Indexed as

Escherichia coliGlycosyltransferasesAnti-Bacterial AgentsBacterial Outer Membrane ProteinsDrug DevelopmentMolecular Docking SimulationMolecular Dynamics SimulationPeptidoglycanAnti-Bacterial AgentsBacterial Outer Membrane ProteinsGlycosyltransferasesPeptidoglycanAntibacterialAntibiotics resistanceEscherichia coliMolecular dynamicsMurGNatural productsVirtual screening

Identifiers

PMID38532068
PMCPMC10966019
OpenAlexW4393196563

What OpenQuestion holds

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LicenceCC BY
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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.