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http://hdl.handle.net/10662/21891
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Campo DC | Valor | idioma |
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dc.contributor.author | Huecas, Sonia | - |
dc.contributor.author | Araújo Bazán, Lidia | - |
dc.contributor.author | Ruiz, Federico M. | - |
dc.contributor.author | Ruiz Ávila, Laura B. | - |
dc.contributor.author | Martínez Vázquez, Rafael Fernando | - |
dc.contributor.author | Escobar Peña, Andrea | - |
dc.contributor.author | Artola, Marta | - |
dc.contributor.author | Vázquez Villa, Henar | - |
dc.contributor.author | Martín Fontecha, Mar | - |
dc.contributor.author | Fernández Tornero, Carlos | - |
dc.contributor.author | López Rodríguez, María L. | - |
dc.contributor.author | Andreu, José M. | - |
dc.date.accessioned | 2024-07-12T11:15:10Z | - |
dc.date.available | 2024-07-12T11:15:10Z | - |
dc.date.issued | 2021-01-03 | - |
dc.identifier.issn | 0022-2623 | - |
dc.identifier.uri | http://hdl.handle.net/10662/21891 | - |
dc.description.abstract | Bacterial resistance to antibiotics makes previously manageable infections again disabling and lethal, highlighting the need for new antibacterial strategies. In this regard, inhibition of the bacterial division process by targeting key protein FtsZ has been recognized as an attractive approach for discovering new antibiotics. Binding of small molecules to the cleft between the N-terminal guanosine triphosphate (GTP)-binding and the C-terminal subdomains allosterically impairs the FtsZ function, eventually inhibiting bacterial division. Nonetheless, the lack of appropriate chemical tools to develop a binding screen against this site has hampered the discovery of FtsZ antibacterial inhibitors. Herein, we describe the first competitive binding assay to identify FtsZ allosteric ligands interacting with the interdomain cleft, based on the use of specific high-affinity fluorescent probes. This novel assay, together with phenotypic profiling and X-ray crystallographic insights, enables the identification and characterization of FtsZ inhibitors of bacterial division aiming at the discovery of more effective antibacterials. | es_ES |
dc.description.sponsorship | This work was supported by grants from the Spanish MECD BFU 2014-51823-R, SAF2016-78792-R, PID2019-106279RB-I00, BFU 2017-87387-P. | es_ES |
dc.format.extent | 16 | es_ES |
dc.format.mimetype | application/pdf | en_US |
dc.language.iso | eng | es_ES |
dc.publisher | ACS Publications | es_ES |
dc.rights | Attribution 4.0 International | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | Fluorescence | es_ES |
dc.subject | Inhibitors | es_ES |
dc.subject | Probes | es_ES |
dc.subject | Fluorescencia | es_ES |
dc.subject | Inhibidores | es_ES |
dc.subject | Sondas | es_ES |
dc.subject | Magnetic properties | es_ES |
dc.subject | Propiedades magnéticas | es_ES |
dc.subject | Screening assays | es_ES |
dc.subject | Ensayos de detección | es_ES |
dc.title | Targeting the FtsZ allosteric binding site with a novel fluorescence polarization screen, cytological and structural approaches for antibacterial discovery | es_ES |
dc.type | article | es_ES |
dc.description.version | peerReviewed | es_ES |
europeana.type | TEXT | en_US |
dc.rights.accessRights | openAccess | es_ES |
dc.subject.unesco | 2306 Química Orgánica | es_ES |
dc.subject.unesco | 2211.17 Propiedades Magnéticas | es_ES |
dc.subject.unesco | 2414.02 Fisiología Bacteriana | es_ES |
europeana.dataProvider | Universidad de Extremadura. España | es_ES |
dc.identifier.bibliographicCitation | Sonia Huecas, Lidia Araújo-Bazán, Federico M. Ruiz, Laura B. Ruiz-Ávila, R. Fernando Martínez, Andrea Escobar-Peña, Marta Artola, Henar Vázquez-Villa, Mar Martín-Fontecha, Carlos Fernández-Tornero, María L. López-Rodríguez, and José M. Andreu Journal of Medicinal Chemistry 2021 64 (9), 5730-5745 DOI: 10.1021/acs.jmedchem.0c02207 | es_ES |
dc.type.version | publishedVersion | es_ES |
dc.contributor.affiliation | CSIC-Centro de Investigaciones Biológicas Margarita Salas | es_ES |
dc.contributor.affiliation | Universidad de Extremadura. Departamento de Química Orgánica e Inorgánica | es_ES |
dc.contributor.affiliation | Universidad Complutense de Madrid | - |
dc.relation.publisherversion | https://pubs.acs.org/doi/10.1021/acs.jmedchem.0c02207 | es_ES |
dc.identifier.doi | 10.1021/acs.jmedchem.0c02207 | - |
dc.identifier.publicationtitle | Journal of Medicinal Chemistry | es_ES |
dc.identifier.publicationissue | 9 | es_ES |
dc.identifier.publicationfirstpage | 5730 | es_ES |
dc.identifier.publicationlastpage | 5745 | es_ES |
dc.identifier.publicationvolume | 64 | es_ES |
dc.identifier.e-issn | 1520-4804 | - |
dc.identifier.orcid | 0000-0002-3278-6074 | es_ES |
Colección: | DQOIN - Artículos |
Archivos
Archivo | Descripción | Tamaño | Formato | |
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acs_jmedchem_0c02207.pdf | 4,82 MB | Adobe PDF | Descargar |
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