Evidence map›Paper›PMID 40591684›Full record

ArticlePloS one2025

A computational study exploring echinoderm-derived compounds for inhibition of aminoglycoside acetyltransferases.

Abdullah R Alanzi, Moneerah J Alqahtani, Jawaher H Alqahtani, Hattan A Alharbi

Abstract read
In one paragraph

Article in PloS one, 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

4 authors.

Abdullah R AlanziDepartment of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia.ORCID https://orcid.org/0009-0000-2565-6573
Moneerah J AlqahtaniDepartment of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia.
Jawaher H AlqahtaniDepartment of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia.
Hattan A AlharbiDepartment of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminoglycoside acetyltransferases (AACs) catalyze the acetylation of aminoglycoside antibiotics, playing a major role in bacterial resistance and posing a serious threat to global healthcare. Despite growing interest in natural products, echinoderm-derived metabolites remain largely unexplored as AAC inhibitors. This study presents a comprehensive in-silico investigation into the potential of these marine compounds to inhibit four key AAC enzymes: Aminoglycoside 2'-N-acetyltransferase, AAC(3)-Ib, AAC(6')-Im, and AAC(3)-Iva. A virtual screening of 1600 echinoderm metabolites was performed using molecular docking, ADMET profiling, and 100 ns molecular dynamics simulations. The top 10 compounds against each enzyme were shortlisted based on binding affinity, with CMNPD15515, CMNPD17440, CMNPD3088, and CMNPD29853 showing the most stable interactions and highest binding energies. These compounds consistently outperformed native aminoglycoside ligands in docking scores and MMGBSA binding free energy calculations, suggesting stronger inhibitory potential. While a few top hits exhibited violations of Lipinski's Rule of Five particularly in molecular weight their strong target engagement and stable dynamic profiles support their candidacy as lead molecules. This work underscores the evolutionary and structural uniqueness of echinoderm metabolites as a promising reservoir for antibiotic adjuvants. It also establishes a computational framework for prioritizing marine natural products against antibiotic resistance targets. Although experimental validation remains essential, this study provides compelling early evidence to guide future in vitro and in vivo research toward the development of novel AAC inhibitors.

Indexed as

AcetyltransferasesEchinodermataEnzyme InhibitorsAminoglycosidesAnimalsAnti-Bacterial AgentsMolecular Docking SimulationMolecular Dynamics SimulationAcetyltransferasesaminoglycoside acetyltransferaseAminoglycosidesAnti-Bacterial AgentsEnzyme Inhibitors

Identifiers

PMID40591684
PMCPMC12212571

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.