Evidence map›Paper›PMID 42644634›Full record

ArticleChembiochem : a European journal of chemical biology2026

Restoring Meropenem Activity Against VIM-1-Producing Klebsiella pneumoniae Through Zinc-Binding Ligands.

Chiara Ragusa, Ruqaiya Khalil, Valentina Giglio, Kaveh Eskandari, Fraser J Scott, Attilio V Vargiu, Graziella Vecchio

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2026. 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

7 authors.

Chiara RagusaDipartimento di Scienze Chimiche, Università degli Studi di Catania, Catania, Italy.ORCID https://orcid.org/0009-0003-6822-481X
Ruqaiya KhalilDepartment of Physics, University of Cagliari, Cagliari, Italy.ORCID https://orcid.org/0000-0002-3440-317X
Valentina GiglioInstitute of Biomolecular Chemistry CNR-ICB, Catania, Italy.ORCID https://orcid.org/0009-0001-0729-3075
Kaveh EskandariDepartment of Pure and Applied Chemistry, University of Strathclyde, Glasgow, Scotland.
Fraser J ScottDepartment of Pure and Applied Chemistry, University of Strathclyde, Glasgow, Scotland.ORCID https://orcid.org/0000-0003-0229-3698
Attilio V VargiuDepartment of Physics, University of Cagliari, Cagliari, Italy.ORCID https://orcid.org/0000-0003-4013-8867
Graziella VecchioDipartimento di Scienze Chimiche, Università degli Studi di Catania, Catania, Italy.ORCID https://orcid.org/0000-0001-8305-081X

Funding

Optimization of efflux avoidance and inhibition for antibiotic developmentR01AI136799 · NIAID · UNIVERSITY OF OKLAHOMA · PI GNANAKARAN, SANDRASEGARAM, RUGGERONE, PAOLO · 2018 to 2022
$5.7M
Fondazione di Sardegna CUP: F23C25000160007National Recovery and Resilience Plan CUP: 85B17000360007National Recovery and Resilience Plan CUP: J85B17000360007NIAID NIH HHS R01 AI136799NIH HHS R01AI136799
6 · The paper itself

Abstract

The growing prevalence of metallo-β-lactamase (MBL)-producing bacteria threatens the clinical efficacy of carbapenems such as meropenem. To investigate potential strategies for restoring β-lactam activity, a panel of compounds was evaluated as putative MBL inhibitors and antibiotic adjuvants. The panel included FDA-approved drugs (carbonic anhydrase inhibitors, an antiviral agent, and a metal chelator), and two novel histidine-pyridine derivatives (D- and L-2-amino-3-(1H-imidazol-4-yl)-N-[2-(pyridin-2-yl)ethyl]propenamides). The latter were synthesized and characterized by NMR spectroscopy and mass spectrometry. Combination assays against Verona Integron-encoded Metallo-β-Lactamase 1 (VIM-1)-producing Klebsiella pneumoniae showed that D-penicillamine and chlorpropamide restored meropenem activity. These effects were supported by time-dependent inhibition and checkerboard assays. Molecular docking and MD simulations with the VIM-1 enzyme further elucidated the putative binding modes of these inhibitors. These results suggest that repurposing the conventional D-penicillamine and chlorpropamide drugs can effectively counteract MBL-mediated resistance.

Indexed as

Anti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-LactamasesKlebsiella pneumoniaeMeropenemZincLigandsMicrobial Sensitivity TestsMolecular Docking SimulationThienamycinsAnti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-LactamasesLigandsMeropenemThienamycinsVIM-1 metallo-beta-lactamaseZincantibioticscarbapenemcarbonic anhydrasechelationchemistrydocking (molecular)K lebsiella pneumoniaemeropenemmicrobiologymolecular dynamics

Identifiers

PMID42644634
PMCPMC13509051

What Socratic 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 Socratic graph.