2024
Durlobactam in combination with β-lactams to combat Mycobacterium abscessus
Shin E, Dousa K, Taracila M, Bethel C, Nantongo M, Nguyen D, Akusobi C, Kurz S, Plummer M, Daley C, Holland S, Rubin E, Bulitta J, Boom W, Kreiswirth B, Bonomo R. Durlobactam in combination with β-lactams to combat Mycobacterium abscessus. Antimicrobial Agents And Chemotherapy 2024, 69: e01174-24. PMID: 39714147, PMCID: PMC11823594, DOI: 10.1128/aac.01174-24.Peer-Reviewed Original ResearchDurlobactam, a Diazabicyclooctane β‑Lactamase Inhibitor, Inhibits BlaC and Peptidoglycan Transpeptidases of Mycobacterium tuberculosis
Nantongo M, Nguyen D, Bethel C, Taracila M, Li Q, Dousa K, Shin E, Kurz S, Nguyen L, Kreiswirth B, Boom W, Plummer M, Bonomo R. Durlobactam, a Diazabicyclooctane β‑Lactamase Inhibitor, Inhibits BlaC and Peptidoglycan Transpeptidases of Mycobacterium tuberculosis. ACS Infectious Diseases 2024, 10: 1767-1779. PMID: 38619138, DOI: 10.1021/acsinfecdis.4c00119.Peer-Reviewed Original ResearchConceptsESI-MSElectrospray ionization mass spectrometryIonization mass spectrometryB-lactamase inhibitorsAcyl-enzyme complexMycobacterial cell wall synthesisMolecular dockingMass spectrometryActive siteInhibit BlaCPeptidoglycan transpeptidaseDiazabicyclooctaneSynthesisAntibiotic susceptibility testingCell wall synthesisInhibition kineticsDrug targetsB-lactamaseDurlobactamSusceptibility testingComplexDockingSpectrometryWall synthesisPeptidoglycan synthesis
2015
Kinetic and Structural Characterization of the Interaction of 6‑Methylidene Penem 2 with the β‑Lactamase from Mycobacterium tuberculosis
Hazra S, Kurz S, Wolff K, Nguyen L, Bonomo R, Blanchard J. Kinetic and Structural Characterization of the Interaction of 6‑Methylidene Penem 2 with the β‑Lactamase from Mycobacterium tuberculosis. Biochemistry 2015, 54: 5657-5664. PMID: 26237118, PMCID: PMC4795174, DOI: 10.1021/acs.biochem.5b00698.Peer-Reviewed Original ResearchConceptsB-lactamaseB-lactamPenem 2Inhibit BlaCActive site residuesB-lactam antibioticsMycobacterium tuberculosisCultures of M. tuberculosisRing openingSite residuesBoronic acidsConstitutive expressionSignificant growth inhibitionStructural characterizationMass spectrometryCompound formsCovalent complexM. tuberculosisGrowth inhibitionBinding inhibitorAcylated formEnzymeRingCompounds
2012
Reappraising the use of β-lactams to treat tuberculosis
Kurz S, Bonomo R. Reappraising the use of β-lactams to treat tuberculosis. Expert Review Of Anti-infective Therapy 2012, 10: 999-1006. PMID: 23106275, PMCID: PMC3728824, DOI: 10.1586/eri.12.96.Peer-Reviewed Original Research
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