ArticleBioorganic & medicinal chemistry letters2019
Profiling interactions of vaborbactam with metallo-β-lactamases.
Article in Bioorganic & medicinal chemistry letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The trial behind it
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Who cites it
20 citing papers in PubMed.
- Restoring Meropenem Activity Against VIM-1-Producing Klebsiella pneumoniae Through Zinc-Binding Ligands.Chembiochem : a European journal of chemical biology · 2026Article
- Susceptibility to novel antimicrobial agents and molecular epidemiology of carbapenem-resistant enterobacterales: a 9-year study in Central China.BMC microbiology · 2026Article
- Machine Learning and Deep Learning Models for Predicting Noncovalent Inhibitors of AmpC β-Lactamase.ACS omega · 2024Article
- Recent Applications of Artificial Intelligence in Discovery of New Antibacterial Agents.Advances and applications in bioinformatics and chemistry : AABC · 2024Review
- Chemical genetic approaches for the discovery of bacterial cell wall inhibitors.RSC medicinal chemistry · 2023Review
- Meropenem/Vaborbactam: β-Lactam/β-Lactamase Inhibitor Combination, the Future in Eradicating Multidrug Resistance.Antibiotics (Basel, Switzerland) · 2023Review
- A review on the mechanistic details of OXA enzymes of ESKAPE pathogens.Pathogens and global health · 2023Review
- Mechanistic Insights to Combating NDM- and CTX-M-Coproducing Klebsiella pneumoniae by Targeting Cell Wall Synthesis and Outer Membrane Integrity.Antimicrobial agents and chemotherapy · 2022Article
- Recent Developments to Cope the Antibacterial Resistance via β-Lactamase Inhibition.Molecules (Basel, Switzerland) · 2022Review
- Imitation of β-lactam binding enables broad-spectrum metallo-β-lactamase inhibitors.Nature chemistry · 2022Article
- Place in Therapy of the Newly Available Armamentarium for Multi-Drug-Resistant Gram-Negative Pathogens: Proposal of a Prescription Algorithm.Antibiotics (Basel, Switzerland) · 2021Review
- Antimicrobial Resistance Conferred by OXA-48 β-Lactamases: Towards a Detailed Mechanistic Understanding.Antimicrobial agents and chemotherapy · 2021Review
- Molecular docking studies, in-silico ADMET predictions and synthesis of novel PEGA-nucleosides as antimicrobial agents targeting class B1 metallo-β-lactamases.In silico pharmacology · 2021Article
- Molecular Basis of Bicyclic Boronate β-Lactamase Inhibitors of Ultrabroad Efficacy - Insights From Molecular Dynamics Simulation Studies.Frontiers in microbiology · 2021Article
- Small Molecule Carboxylates Inhibit Metallo-β-lactamases and Resensitize Carbapenem-Resistant Bacteria to Meropenem.ACS infectious diseases · 2020Article
- Metallo-β-Lactamase Inhibitors Inspired on Snapshots from the Catalytic Mechanism.Biomolecules · 2020Review
- Cyclic boronates as versatile scaffolds for KPC-2 β-lactamase inhibition.RSC medicinal chemistry · 2020Article
- Discovery of Taniborbactam (VNRX-5133): A Broad-Spectrum Serine- and Metallo-β-lactamase Inhibitor for Carbapenem-Resistant Bacterial Infections.Journal of medicinal chemistry · 2020Article
- The latest advances in β-lactam/β-lactamase inhibitor combinations for the treatment of Gram-negative bacterial infections.Expert opinion on pharmacotherapy · 2019Review
- Bicyclic Boronate VNRX-5133 Inhibits Metallo- and Serine-β-Lactamases.Journal of medicinal chemistry · 2019Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
β-Lactams are the most successful antibacterials, yet their use is threatened by resistance, importantly as caused by β-lactamases. β-Lactamases fall into two mechanistic groups: the serine β-lactamases that utilise a covalent acyl-enzyme mechanism and the metallo β-lactamases that utilise a zinc-bound water nucleophile. Achieving simultaneous inhibition of both β-lactamase classes remains a challenge in the field. Vaborbactam is a boronate-based inhibitor that reacts with serine-β-lactamases to form covalent complexes that mimic tetrahedral intermediates in catalysis. Vaborbactam has recently been approved for clinical use in combination with the carbapenem meropenem. Here we show that vaborbactam moderately inhibits metallo-β-lactamases from all 3 subclasses (B1, B2 and B3), with a potency of around 20-100 fold below that by which it inhibits its current clinical targets, the Class A serine β-lactamases. This result contrasts with recent investigations of bicyclic boronate inhibitors, which potently inhibit subclass B1 MBLs but which presently lack activity against B2 and B3 enzymes. These findings indicate that cyclic boronate scaffolds have the potential to inhibit the full range of β-lactamases and justify further work on the development of boronates as broad-spectrum β-lactamase inhibitors.
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Registered trials
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