2021
A human apolipoprotein L with detergent-like activity kills intracellular pathogens
Gaudet RG, Zhu S, Halder A, Kim BH, Bradfield CJ, Huang S, Xu D, Mamiñska A, Nguyen TN, Lazarou M, Karatekin E, Gupta K, MacMicking JD. A human apolipoprotein L with detergent-like activity kills intracellular pathogens. Science 2021, 373 PMID: 34437126, PMCID: PMC8422858, DOI: 10.1126/science.abf8113.Peer-Reviewed Original ResearchMeSH KeywordsApolipoproteins LBacterial Outer MembraneBacteriolysisCell MembraneCell Membrane PermeabilityCells, CulturedCRISPR-Cas SystemsCytosolDetergentsGene EditingGram-Negative BacteriaGTP-Binding ProteinsHumansImmunity, InnateInterferon-gammaLipoproteinsMicrobial ViabilityO AntigensProtein DomainsSalmonella typhimuriumSolubilityConceptsSingle-particle cryo-electron microscopyCell-autonomous defenseCytosol-invasive bacteriaExpression of hundredsNative mass spectrometryCryo-electron microscopyHuman genesDetergent-like activityHost proteinsLipoprotein nanodiscsMammalian lipidsExtracellular transportImmune cytokine interferonCell typesDetergent-like propertiesApolipoprotein LLife-threatening infectionsPotent bactericidal agentsAnionic membranesProteinCytokine interferonNonimmune cellsMass spectrometryCellsMutagenesis
2018
Identifying key membrane protein lipid interactions using mass spectrometry
Gupta K, Li J, Liko I, Gault J, Bechara C, Wu D, Hopper JTS, Giles K, Benesch JLP, Robinson CV. Identifying key membrane protein lipid interactions using mass spectrometry. Nature Protocols 2018, 13: 1106-1120. PMID: 29700483, PMCID: PMC6049616, DOI: 10.1038/nprot.2018.014.Peer-Reviewed Original Research
2017
Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters
Landreh M, Marklund EG, Uzdavinys P, Degiacomi MT, Coincon M, Gault J, Gupta K, Liko I, Benesch JL, Drew D, Robinson CV. Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters. Nature Communications 2017, 8: 13993. PMID: 28071645, PMCID: PMC5234078, DOI: 10.1038/ncomms13993.Peer-Reviewed Original ResearchConceptsIon mobility mass spectrometryGas phaseMass spectrometryMobility mass spectrometryMolecular dynamics simulationsCatalysis rateMD simulationsLipid-binding propertiesDynamics simulationsConformational stabilityStable dimerLarge-scale conformational changesSecondary active transportersConformational changesSpectrometryAntiporter NhaAKingdoms of lifeAnnular lipidsNative foldProtein segmentsInter-domain contactsRole of lipidsThermus thermophilusMembrane lipidsNHA2
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 ResearchHigh-resolution mass spectrometry of small molecules bound to membrane proteins
Gault J, Donlan JA, Liko I, Hopper JT, Gupta K, Housden NG, Struwe WB, Marty MT, Mize T, Bechara C, Zhu Y, Wu B, Kleanthous C, Belov M, Damoc E, Makarov A, Robinson CV. High-resolution mass spectrometry of small molecules bound to membrane proteins. Nature Methods 2016, 13: 333-336. PMID: 26901650, PMCID: PMC4856209, DOI: 10.1038/nmeth.3771.Peer-Reviewed Original Research
2012
Lipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins
Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P. Lipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins. Journal Of The American Society For Mass Spectrometry 2012, 23: 1716-1728. PMID: 22847390, DOI: 10.1007/s13361-012-0437-4.Peer-Reviewed Original ResearchConceptsHigh-performance liquid chromatographyMass spectrometryIonization mass spectrometric studyHigh-resolution mass spectrometryDiagnostic fragment ionsResolution mass spectrometryMass spectrometric characterizationMass spectrometric studyChain length variationReversed-phase high-performance liquid chromatographyMS/MS analysisLaser desorption ionizationMass spectrometric analysisLinear precursorsFragment ionsMacrocyclic ringFatty acid chainsPerformance liquid chromatographySpectrometric characterizationGlu replacementSpectrometric studyAcid moietyComplex mixturesDesorption ionizationFatty acid moieties
2010
Disulfide Bond Assignments by Mass Spectrometry of Native Natural Peptides: Cysteine Pairing in Disulfide Bonded Conotoxins
Gupta K, Kumar M, Balaram P. Disulfide Bond Assignments by Mass Spectrometry of Native Natural Peptides: Cysteine Pairing in Disulfide Bonded Conotoxins. Analytical Chemistry 2010, 82: 8313-8319. PMID: 20843009, DOI: 10.1021/ac101867e.Peer-Reviewed Original ResearchConceptsS bond cleavageBond cleavageNatural peptidesDisulfide bondsProduct ion yieldsMass spectral fragmentationDisulfide bond assignmentsDisulfide pairingFragment ionsStructure elucidationPeptide backboneBond assignmentDissociation conditionsMass spectrometryMultiple disulfide bondsCysteine pairingsSpectral fragmentationPossible disulfideMultiple cysteine residuesNative peptideAnalytical methodologyBondsCorrect disulfide pairingIon yieldFurther fragmentation