ArticleACS medicinal chemistry letters2015
Azolylthioacetamide: A Highly Promising Scaffold for the Development of Metallo-β-lactamase Inhibitors.
Article in ACS medicinal chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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.
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.
Who cites it
19 citing papers in PubMed.
- In Silico Evaluation of Potential NDM-1 Inhibitors: An Integrated Docking and Molecular Dynamics Approach.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases.Journal of enzyme inhibition and medicinal chemistry · 2024Review
- Identification of Benzothiazoles Bearing 1,3,4-Thiadiazole as Antiproliferative Hybrids Targeting VEGFR-2 and BRAF Kinase: Design, Synthesis, BIO Evaluation and In Silico Study.Molecules (Basel, Switzerland) · 2024Article
- New benzothiazole hybrids as potential VEGFR-2 inhibitors: design, synthesis, anticancer evaluation, andJournal of enzyme inhibition and medicinal chemistry · 2023Article
- A Modified Vancomycin Molecule Confers Potent Inhibitory Efficacy against Resistant Bacteria Mediated by Metallo-β-Lactamases.Molecules (Basel, Switzerland) · 2022Article
- Efficient synthesis, biological evaluation, and docking study of isatin based derivatives as caspase inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2020Article
- Discovery and characterization of New Delhi metallo-β-lactamase-1 inhibitor peptides that potentiate meropenem-dependent killing of carbapenemase-producing Enterobacteriaceae.The Journal of antimicrobial chemotherapy · 2020Article
- Binding of 2-(Triazolylthio)acetamides to Metallo-β-lactamase CcrA Determined with NMR.ACS omega · 2020Article
- Synthesis of New Planar-Chiral Linked [2.2]Paracyclophanes-Molecules (Basel, Switzerland) · 2020Article
- Article
- Kinetic, Thermodynamic, and Crystallographic Studies of 2-Triazolylthioacetamides as Verona Integron-Encoded Metallo-β-Lactamase 2 (VIM-2) Inhibitor.Biomolecules · 2020Article
- Discovery of [1,2,4]Triazole Derivatives as New Metallo-β-Lactamase Inhibitors.Molecules (Basel, Switzerland) · 2019Article
- Halogen-Substituted Triazolethioacetamides as a Potent Skeleton for the Development of Metallo-β-Lactamase Inhibitors.Molecules (Basel, Switzerland) · 2019Article
- Azolylthioacetamides as potential inhibitors of New Delhi metallo-β-lactamase-1 (NDM-1).The Journal of antibiotics · 2019Article
- β-lactam/β-lactamase inhibitor combinations: an update.MedChemComm · 2018Review
- Discovery of a Novel Metallo-β-Lactamase Inhibitor That Potentiates Meropenem Activity against Carbapenem-Resistant Enterobacteriaceae.Antimicrobial agents and chemotherapy · 2018Article
- Carbamylmethyl Mercaptoacetate Thioether: A Novel Scaffold for the Development of L1 Metallo-β-lactamase Inhibitors.ACS medicinal chemistry letters · 2017Article
- The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Triazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo-β-Lactmase-1 (NDM-1) Inhibitors.ACS medicinal chemistry letters · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new scaffold, azolylthioacetamide, was constructed and assayed against metallo-β-lactamases (MβLs). The obtained molecules specifically inhibited MβL ImiS, and 1c was found to be the most potent inhibitor, with a K i = 1.2 μM using imipenem as substrate. Structure-activity relationships reveal that the aromatic carboxyl improves inhibitory activity of the inhibitors, but the aliphatic carboxyl does not. Compounds 1c-d and 1h-i showed the best antibacterial activities against E. coli BL21(DE3) cells producing CcrA or ImiS, resulting in 32- and 8-fold reduction in MIC values, respectively; 1c and 1f-j resulted in a reduction in MIC against P. aeruginosa. Docking studies revealed that 1a, 1c, and 1d fit tightly into the substrate binding site of CphA as a proxy for ImiS with the aromatic carboxylate forming interactions with Lys224, the Zn(II) ion, the backbone of Asn233, and hydrophobic portions of the inhibitors aligning with hydrophobic patches of the protein surface.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.