Evidence map›Paper›PMID 41134396›Full record

ArticleCurrent microbiology2025

Antibacterial Activity of Chalcone (2E)-3-({4-[(2E)-3-(4-Nitrophenyl) prop-2-enol] phenyl}carbamoyl) prop-2-enoic acid and Its Effect Against Staphylococcus aureus Carrying Efflux Pump and β-Lactamase.

Olivia Caroline Maia de Moura, Júlio César Silva, Raimundo Luiz Silva Pereira, Isaac Moura Araújo, Sheila Alves Gonçalves, João Arthur de Oliveira Borges, Daniel Sampaio Alves, Gabriel Gonçalves Alencar, Thiago Sampaio de Freitas, Vanessa Lima-Bezerra and 7 more

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Article in Current microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

17 authors.

Olivia Caroline Maia de MouraFederal University of Cariri-UFCA, Crato, CE, Brazil.
Júlio César SilvaFederal University of Cariri-UFCA, Crato, CE, Brazil.
Raimundo Luiz Silva PereiraRegional University of Cariri-URCA, Crato, CE, Brazil.
Isaac Moura AraújoRegional University of Cariri-URCA, Crato, CE, Brazil.
Sheila Alves GonçalvesRegional University of Cariri-URCA, Crato, CE, Brazil.
João Arthur de Oliveira BorgesRegional University of Cariri-URCA, Crato, CE, Brazil.
Daniel Sampaio AlvesRegional University of Cariri-URCA, Crato, CE, Brazil.
Gabriel Gonçalves AlencarRegional University of Cariri-URCA, Crato, CE, Brazil.
Thiago Sampaio de FreitasRegional University of Cariri-URCA, Crato, CE, Brazil.
Vanessa Lima-BezerraFederal University of Cariri-UFCA, Crato, CE, Brazil.
Walber Henrique Ferreira RibeiroCenter for Exact Sciences and Technology-Chemistry Course, Vale do Acaraú University, Sobral, CE, Brazil.
Francisco Ferdinando Mesquita CajazeirasCenter for Exact Sciences and Technology-Chemistry Course, Vale do Acaraú University, Sobral, CE, Brazil.
Jesyka Macedo GuedesCenter for Exact Sciences and Technology-Chemistry Course, Vale do Acaraú University, Sobral, CE, Brazil.
Paulo Nogueira BandeiraCenter for Exact Sciences and Technology-Chemistry Course, Vale do Acaraú University, Sobral, CE, Brazil.
Hélcio Silva Dos SantosRegional University of Cariri-URCA, Crato, CE, Brazil.
Henrique Douglas Melo CoutinhoRegional University of Cariri-URCA, Crato, CE, Brazil.
Francisco Nascimento Pereira JuniorFederal University of Cariri-UFCA, Crato, CE, Brazil. francisco.pereira@ufca.edu.br.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent years, the emergence and propagation of resistant microorganisms have outpaced the introduction of new therapeutic alternatives capable of combating them, giving rise to concerns about an imminent global health crisis caused by infectious diseases. Among the various resistance mechanisms bacteria employ, efflux pumps and β-lactamase enzymes are particularly significant. Consequently, numerous studies have been conducted to identify novel therapeutic alternatives with antibacterial activity and the capacity to inactivate these mechanisms. In this study, a novel (2E)-3-({4-[(2E)-3-(4-nitrophenyl) prop-2-enol] phenyl} carbamoyl) prop-2-enoic acid chalcone, termed CAP, was synthesised. Despite the CAP chalcone exhibiting no direct antibacterial activity and being ineffective against the efflux pump present in the K2068 strain, it was found to potentiate the action of ampicillin when associated with this antibiotic in the K4100 strain, which carries the β-lactamase mechanism. This finding suggests that the chalcone in question could act by inhibiting the resistance mechanism mediated by these enzymes.

Indexed as

Anti-Bacterial AgentsBacterial Proteinsbeta-LactamasesChalconesMembrane Transport ProteinsStaphylococcus aureusAmpicillinMicrobial Sensitivity TestsAmpicillinAnti-Bacterial AgentsBacterial Proteinsbeta-LactamasesChalconesMembrane Transport Proteins

Identifiers

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Registered trials

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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.