2025
P-788. Exploring β-Lactam Interactions with DacB1: Unraveling Optimal Therapies for Combating Drug-Resistant Mycobacterium tuberculosis
Nantongo M, Nguyen D, Shin E, Bethel C, Taracila M, Dousa K, Kurz S, Nguyen L, Kreiswirth B, Boom W, Bonomo R. P-788. Exploring β-Lactam Interactions with DacB1: Unraveling Optimal Therapies for Combating Drug-Resistant Mycobacterium tuberculosis. Open Forum Infectious Diseases 2025, 12: ofae631.982. PMCID: PMC11778675, DOI: 10.1093/ofid/ofae631.982.Peer-Reviewed Original ResearchMinimum inhibitory concentrationAcyl-enzyme adductOxyanion holeB-lactamB-lactamasePeptidoglycan synthesis pathwayCarbonyl groupHydrophobic interactionsElectrospray ionization mass spectrometryAcyl-enzyme formationB-lactam antibioticsMichaelis-Menten complexC1‐methyl groupProtein motifsPeptidoglycan biosynthesisDrug-resistant Mycobacterium tuberculosisIonization mass spectrometryPeptidoglycan synthesisD-carboxypeptidaseAnalysis of meropenemB-lactamase inhibitorsClinical isolatesBroth microdilutionClinically achievable concentrationsSynthesis pathway
2024
Durlobactam, 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
2016
Mass spectrometric analysis of dimer-disrupting mutations in Plasmodium triosephosphate isomerase
Bandyopadhyay D, Prakash S, Gupta K, Balaram P. Mass spectrometric analysis of dimer-disrupting mutations in Plasmodium triosephosphate isomerase. Analytical Biochemistry 2016, 500: 45-50. PMID: 26919806, DOI: 10.1016/j.ab.2016.02.011.Peer-Reviewed Original Research
2001
A Mass Spectrometric Labeling Strategy for High‐Throughput Reaction Evaluation and Optimization: Exploring C−H Activation
Szewczyk JW, Zuckerman RL, Bergman RG, Ellman JA. A Mass Spectrometric Labeling Strategy for High‐Throughput Reaction Evaluation and Optimization: Exploring C−H Activation. Angewandte Chemie International Edition 2001, 40: 216-219. PMID: 29711936, DOI: 10.1002/1521-3773(20010105)40:1<216::aid-anie216>3.0.co;2-k.Peer-Reviewed Original ResearchPositive ion electrospray ionization mass spectrometryIon electrospray ionization mass spectrometryElectrospray ionization mass spectrometryIonization mass spectrometry
1997
Detection and Identification of Transient Enzyme Intermediates Using Rapid Mixing, Pulsed-Flow Electrospray Mass Spectrometry †
Paiva A, Tilton R, Crooks G, Huang L, Anderson K. Detection and Identification of Transient Enzyme Intermediates Using Rapid Mixing, Pulsed-Flow Electrospray Mass Spectrometry †. Biochemistry 1997, 36: 15472-15476. PMID: 9398276, DOI: 10.1021/bi971883i.Peer-Reviewed Original ResearchConceptsTetrahedral intermediateElectrospray ionization ion trap mass spectrometerIon trap mass spectrometerNegative ion mass spectraElectrospray ionization mass spectrometryCollision-induced dissociationEnzyme intermediateIon mass spectraTrap mass spectrometerIonization mass spectrometryEnzyme reaction intermediatesElectrospray ionizationDaughter ionsSubsecond time scaleEnzyme active siteReaction intermediatesAtomic mass unitsMass spectraMass spectrometerChemical quench studiesQuenching studiesMass spectrometryRapid mixing deviceQuenching methodActive site
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