http://repositorio.unb.br/handle/10482/46916
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Título : | α-Alkylidene δ-lactones inhibit quorum sensing phenotypes in Chromobacterium strain CV026 showing interaction with the CviR receptor |
Autor : | Favero, Fernanda Tolentino, Terezinha Alves Fernandes, Vinicius Treptow, Werner Pereira, Alex Leite Machado, Angelo Henrique Lira |
metadata.dc.identifier.orcid: | https://orcid.org/0000-0003-4284-9929 |
Assunto:: | Bactérias Lactonas |
Fecha de publicación : | 15-jun-2023 |
Editorial : | The Royal Society of Chemistry |
Citación : | FAVERO, Fernanda et al. α-Alkylidene δ-lactones inhibit quorum sensing phenotypes in Chromobacterium strain CV026 showing interaction with the CviR receptor. RSC Advances, [S. l.], v. 13, p. 18045-18057, 2023. DOI: https://doi.org/10.1039/D3RA01975F. Disponível em: https://pubs.rsc.org/en/content/articlelanding/2023/ra/d3ra01975f. Acesso em: 27 nov. 2023. |
Abstract: | Disruption of bacterial quorum sensing (QS) is presented as a promising strategy to overcome clinically relevant and phytopathogenic bacteria. This work presents α-alkylidene δ-lactones as new chemical scaffolds that inhibit the biosynthesis of violacein in the biosensor strain Chromobacterium CV026. Three molecules displayed higher than 50% violacein reduction when tested at concentrations lower than 625 µM. The most active α-alkylidene δ-lactone inhibited the hydrolysis of chitin concomitantly with the inhibition of violacein production in CV026, suggesting the disruption of its QS machinery. Further, RT-qPCR and competition experiments showed this molecule to be a transcriptional inhibitor of the QS-regulated operon vioABCDE. Docking calculations suggested a good correlation between binding affinity energies and inhibition effects, with all molecules positioned within the CviR autoinducer-binding domain (AIBD). The most active lactone yielded the best binding affinity energy, most probably due to its unprecedented binding with the AIBD. Our results show α-alkylidene δ-lactones as promising chemical scaffolds for the development of new QS inhibitors affecting LuxR/LuxI-systems. |
metadata.dc.description.unidade: | Instituto de Química (IQ) Faculdade UnB Ceilândia (FCE) Instituto de Ciências Biológicas (IB) Departamento de Biologia Celular (IB CEL) |
Licença:: | (CC BY NC) This article is licensed under aCreative Commons Attribution-NonCommercial 3.0 Unported Licence. |
DOI: | https://doi.org/10.1039/D3RA01975F |
Aparece en las colecciones: | Artigos publicados em periódicos e afins |
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