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Metallo-β-lactamase inhibitors inspired on snapshots from the catalytic mechanism

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dc.citation.titleBiomoleculeses
dc.citation.volume10(6)es
dc.creatorPalacios, Antonela R.
dc.creatorRossi, María Agustina
dc.creatorMahler, Graciela S.
dc.creatorVila, Alejandro J.
dc.date.accessioned2021-04-09T19:50:47Z
dc.date.available2021-04-09T19:50:47Z
dc.date.issued2020-06-03
dc.descriptionβ-Lactam antibiotics are the most widely prescribed antibacterial drugs due to their low toxicity and broad spectrum. Their action is counteracted by different resistance mechanisms developed by bacteria. Among them, the most common strategy is the expression of β-lactamases, enzymes that hydrolyze the amide bond present in all β-lactam compounds. There are several inhibitors against serine-β-lactamases (SBLs). Metallo-β-lactamases (MBLs) are Zn(II)-dependent enzymes able to hydrolyze most β-lactam antibiotics, and no clinically useful inhibitors against them have yet been approved. Despite their large structural diversity, MBLs have a common catalytic mechanism with similar reaction species. Here, we describe a number of MBL inhibitors that mimic different species formed during the hydrolysis process: substrate, transition state, intermediate, or product. Recent advances in the development of boron-based and thiol-based inhibitors are discussed in the light of the mechanism of MBLs. We also discuss the use of chelators as a possible strategy, since Zn(II) ions are essential for substrate binding and catalysis.es
dc.descriptionPara citar este articulo: Palacios, A.R.; Rossi, M.-A.; Mahler, G.S.; Vila, A.J. Metallo-β-Lactamase Inhibitors Inspired on Snapshots from the Catalytic Mechanism. Biomolecules 2020, 10, 854. https://doi.org/10.3390/biom10060854
dc.description.filFil: Palacios, Antonela R. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.es
dc.description.filFil: Rossi, María Agustina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.es
dc.description.filFil: Mahler, Graciela S. Universidad de la Republica. Facultad de Química. Laboratorio de Química Farmacéutica; Uruguay.es
dc.description.filFil: Vila, Alejandro J. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.es
dc.description.filFil: Vila, Alejandro J. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Área Biofísica; Argentina.es
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica (ANPCyT): PICT-2016-1657es
dc.description.sponsorshipNational Institutes of Health (NIH): NIAID, 2R01AI100560-06A1es
dc.formatapplication/pdf
dc.format.extent1-34es
dc.identifier.issn2218-273Xes
dc.identifier.urihttp://hdl.handle.net/2133/20476
dc.language.isoenges
dc.publisherMDPIes
dc.relation.publisherversionhttps://www.mdpi.com/2218-273X/10/6/854es
dc.relation.publisherversionhttps://doi.org/10.3390/biom10060854es
dc.rightsopenAccesses
dc.rights.holderPalacios, Antonela R.es
dc.rights.holderRossi, María Agustinaes
dc.rights.holderMahler, Graciela S.es
dc.rights.holderVila, Alejandro J.es
dc.rights.holderUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticases
dc.rights.textAttribution 4.0 International (CC BY 4.0)es
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subjectMetallo-β-lactamaseses
dc.subjectMechanism-based Inhibitorses
dc.subjectDrug Resistance, Microbiales
dc.subjectReaction Mechanismes
dc.titleMetallo-β-lactamase inhibitors inspired on snapshots from the catalytic mechanismes
dc.titleMetallo-beta-lactamase inhibitors inspired on snapshots from the catalytic mechanismes
dc.typearticle
dc.typeartículo
dc.typepublishedVersion
dc.type.collectionarticulo
dc.type.versionpublishedVersiones

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