ArticleChembiochem : a European journal of chemical biology2026
Restoring Meropenem Activity Against VIM-1-Producing Klebsiella pneumoniae Through Zinc-Binding Ligands.
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.
What it found
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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.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Restoring Meropenem Activity Against VIM-1-Producing Klebsiella pneumoniae Through Zinc-Binding Ligands.Chembiochem : a European journal of chemical biology · 2026Article
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Authors and funding
7 authors.
Funding
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.
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Registered trials
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