Journal of the American Society for Mass Spectrometry最新文献

Differentiation of Isomeric Bis(monoacylglycero)phosphates and Phosphatidylglycerols via Gas-Phase Ion/Ion Reactions and Ion Trap Collision-Induced Dissociation 通过气相离子/离子反应和离子阱碰撞诱导解离分化同分异构体二（单酰基甘油）磷酸和磷脂酰甘油

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-08-13 DOI: 10.1021/jasms.6c00236

Rebekah G. Bogle, Sarah T. Nsiah, De’Shovon M. Shenault, Katherine A. Walker, Caitlin E. Randolph, Scott A. McLuckey

{"title":"Differentiation of Isomeric Bis(monoacylglycero)phosphates and Phosphatidylglycerols via Gas-Phase Ion/Ion Reactions and Ion Trap Collision-Induced Dissociation","authors":"Rebekah G. Bogle, Sarah T. Nsiah, De’Shovon M. Shenault, Katherine A. Walker, Caitlin E. Randolph, Scott A. McLuckey","doi":"10.1021/jasms.6c00236","DOIUrl":"https://doi.org/10.1021/jasms.6c00236","url":null,"abstract":"Bis(monoacylglycero)phosphates (BMPs) and phosphatidylglycerols(PGs) constitute a unique class of lipid regioisomers with distinctstructural features and biochemical roles. However, ion trap collision-induceddissociation (IT-CID) alone is insufficient to differentiate isomericdeprotonated PG and BMP ions. Herein, we describe a gas-phase charge-inversionion/ion reaction that generates an ion type enabling straightforward,unambiguous differentiation of BMP and PG isomers upon IT-CID. Theapproach involves charge inversion of isomeric, deprotonated BMP orPG anions using the dicationic magnesium 4,4′,4″-tri-tert-butyl-2,2′:6′,2″-terpyridine complex([Mg(ttbt)2]2+), followed by IT-CID to producediagnostic fragment ions indicative of each isomer. These fragmentions arise from even-electron charge remote fragmentation (CRF) pathways.Subsequent MSn experiments involving fatty acid fragmentions complexed with [Mg(ttbt)2]2+ proceed throughodd-electron radical directed dissociation (RDD), providing detailedinformation on acyl chain carbon–carbon double bond position(s).Ion types generated via negative ion mode nESI and through ion/ionreactions were applied to distinguish targeted PG and BMP isomersat the carbon–carbon double bond positional level in a mouseliver extract using a shotgun lipidomics approach.","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 9","pages":"2192–2200"},"PeriodicalIF":2.9,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148870313","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural Elucidation of Fc- and Fab-Associated N-Glycans in Cetuximab Using Protein A-Assisted Domain-Resolved Glycan Profiling Using Mass Spectrometry 利用蛋白a辅助结构域解析聚糖谱分析西妥昔单抗中Fc-和fab -相关n-聚糖的结构解析。

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-07-06 DOI: 10.1021/jasms.6c00136

Divya Chauhan, Tarun Shivach, Anurag S. Rathore

{"title":"Structural Elucidation of Fc- and Fab-Associated N-Glycans in Cetuximab Using Protein A-Assisted Domain-Resolved Glycan Profiling Using Mass Spectrometry","authors":"Divya Chauhan, Tarun Shivach, Anurag S. Rathore","doi":"10.1021/jasms.6c00136","DOIUrl":"10.1021/jasms.6c00136","url":null,"abstract":"Glycosylation of monoclonal antibodies is a key determinantoftheir efficacy, stability, and safety, requiring analytical methodscapable of resolving site-specific heterogeneity with high sensitivity.In this work, we present a Protein A-assisted, domain-resolved glycanprofiling approach for the mass spectrometry-based structural elucidationand quantification of N-glycans linked to Fc andFab in cetuximab. Antibody domains were selectively extracted usingProtein A affinity separation, allowing for independent enzymaticrelease of N-glycans from Fc and Fab sections, followedby high-resolution mass spectrometry for detailed glycan profilingand comparative characterization of Fc- and Fab-associated glycanpopulations. In comparison to conventional total glycan analysis,our technique decreases spectral complexity and allows for obviousdistinction of domain-specific glycosylation patterns. Crucially,domain-specific released glycan profiling improves the detection andprecise measurement of low-abundance glycoforms, such as sialylated,high-mannose, and afucosylated species that frequently remain hiddenin conventional approaches. The proposed approach facilitates domain-specificcharacterization of glycan distributions across antibody regions byreducing analytical complexity and improving interpretation of Fc-and Fab-associated glycosylation patterns. Our results show that areliable and repeatable platform for thorough, domain-level glycancharacterization and quantification is available, supporting applicationsin quality control and biosimilar comparability studies, and in generalduring biopharmaceutical development.","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 9","pages":"2094–2102"},"PeriodicalIF":2.9,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148395214","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Quantifying Protein Temporal Changes with Mass Spectrometry in Plasma Samples from Breast Cancer Patients Undergoing Radiotherapy 质谱法定量乳腺癌放疗患者血浆样品中蛋白质时间变化

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-07-25 DOI: 10.1021/jasms.6c00168

Kathryn L. Kapp, Catherine C. Going, Fernando J. Garcia-Marques, Ke Leow, Alisha Maltos, Abel Bermudez, Marta Vilalta, Marjan Rafat, Melissa Jenkins, Jie Jane Chen, Parag Mallick, Kathleen Horst, Edward Graves, Sharon J. Pitteri

{"title":"Quantifying Protein Temporal Changes with Mass Spectrometry in Plasma Samples from Breast Cancer Patients Undergoing Radiotherapy","authors":"Kathryn L. Kapp, Catherine C. Going, Fernando J. Garcia-Marques, Ke Leow, Alisha Maltos, Abel Bermudez, Marta Vilalta, Marjan Rafat, Melissa Jenkins, Jie Jane Chen, Parag Mallick, Kathleen Horst, Edward Graves, Sharon J. Pitteri","doi":"10.1021/jasms.6c00168","DOIUrl":"10.1021/jasms.6c00168","url":null,"abstract":"Radiation therapy (RT) is a central component of cancertreatment,including breast cancer, and primarily damages DNA in cancer cells,causing cell death. However, secondary effects of RT that may influencetumor and normal tissue both within and beyond the site of irradiationare not well characterized, particularly at the level of the circulatingblood proteome. In this study, isotopic acrylamide labeling of proteinsand high-resolution LC–MS/MS were used to analyze plasma proteinsfrom breast cancer patients before, during, and after RT. Clusteringanalysis was used to group proteins according to how their levelschanged over time. A total of 31 proteins were identified whose levelswere altered during RT but returned to baseline following the conclusionof treatment, representing key parts of the immune response to RT.Another set of 31 proteins related to the extracellular matrix andother functions was altered during RT and remained altered after RT.Specific time points were also examined, and acute changes were identifiedat the start of RT in the levels of 63 proteins involved in coagulation,cell–cell adhesion, and carbohydrate metabolism. After theend of RT, the circulating levels of 23 extracellular matrix proteinsremained altered. These LC–MS/MS findings were validated orthogonallyby ELISAs of three proteins in a larger group of breast cancer patientsundergoing RT. Overall, in this study, temporal changes in the circulatingblood proteome of breast cancer patients undergoing RT were characterized,and these altered protein levels were linked to potential alterationsin biological pathways.","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 9","pages":"2141–2154"},"PeriodicalIF":2.9,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148590092","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Correction to “Mass Spectrometry-Driven Epitope Mapping: Application of Diethylpyrocarbonate Covalent Labeling for the Immunotherapeutic Target Programmed Cell Death Protein 1” 修正“质谱驱动的表位定位：焦碳酸二乙基共价标记在免疫治疗靶细胞程序性死亡蛋白1中的应用”

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-08-18 DOI: 10.1021/jasms.6c00328

Parawan Ramanandana, Phumrapee Pianpaktr, Jiradej Makjaroen, Tossapon Wongtangprasert, Zachary J. Kirsch, Eric M. Graban, Richard W. Vachet, Poorichaya Somparn, Trairak Pisitkun, Patanachai K. Limpikirati

引用次数: 0

Characterizing the Compensation Voltage Landscape for Label-Free and TMTpro-Derivatized Peptides in FAIMS-Coupled Proteomics 在faims偶联蛋白质组学中表征无标签肽和tmtpro衍生肽的补偿电压格局

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-08-13 DOI: 10.1021/jasms.6c00208

Christopher D. McGann, Joao A. Paulo

引用次数: 0

High-Throughput Proteomic and Glycoproteomic Analyses in Benign Prostatic Hyperplasia 良性前列腺增生的高通量蛋白质组学和糖蛋白质组学分析

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-08-04 DOI: 10.1021/jasms.6c00143

Feixuan Wu, Alexis E. Adrian, Allen Zhao, Han Zhang, Peng-Kai Liu, Yajing Lu, Douglas W. Strand, William A. Ricke, Lingjun Li

{"title":"High-Throughput Proteomic and Glycoproteomic Analyses in Benign Prostatic Hyperplasia","authors":"Feixuan Wu, Alexis E. Adrian, Allen Zhao, Han Zhang, Peng-Kai Liu, Yajing Lu, Douglas W. Strand, William A. Ricke, Lingjun Li","doi":"10.1021/jasms.6c00143","DOIUrl":"https://doi.org/10.1021/jasms.6c00143","url":null,"abstract":"Benign prostatic hyperplasia (BPH) is a disease affectingthe majorityof aging men; 90% of men develop histological BPH by the time theyreach their eighties. BPH can lead to bothersome lower urinary tractsymptoms (LUTS), which may reduce quality of life. Many patients failcurrent treatment options and may progress to surgical intervention.Furthermore, diagnosis is reliant on symptom questionnaires and thecause of LUTS can be difficult to distinguish. Currently, BPH canonly be definitively diagnosed through histological analysis of prostatetissue, which is not the standard of care. The resulting lack of clinicaltissue samples is a major limitation in investigating disease pathology.Improved understanding of disease development and progression, alongwith objective biomarkers of disease, is needed for BPH. This investigationuses mass spectrometry (MS)-based proteomics and glycoproteomics tocompare healthy prostate tissue with prostate tissue affected by BPHto address this gap in knowledge. By integrating proteomics and glycoproteomics,we identified 206 proteins and 44 glycopeptides that were significantlyaltered between BPH and control samples. These findings provide deeperinsight into disease-associated pathways and may facilitate the identificationof clinically relevant targets for further investigation.","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 9","pages":"2103–2111"},"PeriodicalIF":2.9,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148870421","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Integrating Computational Chemistry and Ion Mobility Spectrometry into Non-Targeted Analysis Workflows for the Structural Elucidation of Emerging PFAS 将计算化学和离子迁移谱法集成到新兴PFAS结构解析的非靶向分析工作流程中

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-08-21 DOI: 10.1021/jasms.6c00201

Allison N. Fry, Christian Ieritano, W. Scott Hopkins, P. B. Armentrout, James N. Dodds, Erin S. Baker

{"title":"Integrating Computational Chemistry and Ion Mobility Spectrometry into Non-Targeted Analysis Workflows for the Structural Elucidation of Emerging PFAS","authors":"Allison N. Fry, Christian Ieritano, W. Scott Hopkins, P. B. Armentrout, James N. Dodds, Erin S. Baker","doi":"10.1021/jasms.6c00201","DOIUrl":"https://doi.org/10.1021/jasms.6c00201","url":null,"abstract":"Per-and polyfluoroalkyl substances (PFAS) are an evolvingclassof synthetic chemicals that are pervasive in the environment due towidespread manufacturing and consumer use, such that PFAS contaminationis of great concern. Although thousands of PFAS structures have beenreported to date, this number increases daily with the identificationof new PFAS from advances in non-targeted analysis (NTA) workflows.Ion mobility spectrometry in combination with mass spectrometry (IMS-MS)has recently been incorporated into PFAS NTA studies. Although MSprovides essential precursor and fragmentation data, IMS offers complementarystructural information via the measurement of the ion-neutral collisioncross section (CCS) values. Experimental CCS values can then be comparedwith those calculated in silico from candidate 3Dstructures to meet confidence-level criteria in analyte assignmentswithin NTA workflows. Although this approach has been applied sincethe late 1990s, PFAS often exhibited poorer agreement between thecalculated and experimental CCS values. To address this limitation,we propose an optimized computational workflow to calculate Boltzmann-weightedCCS values for PFAS structures generated via quantum-chemical calculations.This workflow was assessed with experimental CCS values from 56 knownPFAS structures across seven classes and resulted in an average percenterror of 2.0%. Moreover, 11 new PFAS structures were proposed fromNTA, with average errors of 1.3%. The combination of this new computationalworkflow and experimental IMS-MS measurements therefore establishesa workflow for structural elucidation of emerging PFAS.","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 9","pages":"2168–2178"},"PeriodicalIF":2.9,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148877878","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Linkage between Quaternary Structure and Subunit Sequencing of Zebra Finch Hemoglobin via Hyphenation of Size Exclusion Chromatography with Native Top-Down Mass Spectrometry 通过尺寸排除色谱-自顶向下质谱联用技术研究斑胸草雀血红蛋白的四级结构和亚基测序。

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-06-19 DOI: 10.1021/jasms.6c00041

Léa Letissier, Corentin Beaumal, Turkan Nabiyeva, François Criscuolo, Fabrice Bertile, Christine Schaeffer-Reiss, Sarah Cianférani, Oscar Hernandez-Alba

{"title":"Linkage between Quaternary Structure and Subunit Sequencing of Zebra Finch Hemoglobin via Hyphenation of Size Exclusion Chromatography with Native Top-Down Mass Spectrometry","authors":"Léa Letissier, Corentin Beaumal, Turkan Nabiyeva, François Criscuolo, Fabrice Bertile, Christine Schaeffer-Reiss, Sarah Cianférani, Oscar Hernandez-Alba","doi":"10.1021/jasms.6c00041","DOIUrl":"10.1021/jasms.6c00041","url":null,"abstract":"Hemoglobinis the protein responsible for oxygen transport in manyvertebrates, and any structural alteration can lead to health issues.Although well characterized in humans, it is less known for birds.Studies have reported the identification of several α subunitsalong with the presence of endogenous cofactors in different avianerythrocytes. However, the native structure of avian hemoglobin remainselusive. Native top-down mass spectrometry (nTD-MS) offers powerfulinsights into biomolecular complexes, providing information on quaternarystructure, subunit connectivity, stoichiometry, and subunit sequences.However, most nTD-MS approaches use direct infusion, which can limitthe multiprotein complex population characterization. Here, we reporton the development of a size-exclusion-chromatography (SEC) nTD-MSapproach, including different activation methods to characterize thezebra finch hemoglobin structure. Three different tetramer populationswere separated and characterized using optimized pMS2 (pseudo-MS2, complex-up) workflows to induce subunit and endogenous cofactorrelease previously reported by our group. The analytical strategywas improved with the addition of an extra level of characterizationthrough the implementation of a pMS3 (pseudo-MS3, complex-down) step with controlled pressure, allowing almost completesequence coverage of all the subunits (>94%), along with the identificationof inositol pentaphosphate as a cofactor of the tetramer structure.Altogether, these results pinpoint the key role of SEC-nTD-MS workflowsto enable a complete structural characterization of hemoglobin complexes,which could provide crucial information regarding oxygen affinity,bird environment adaptation, or phylogeny.","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 9","pages":"2060–2071"},"PeriodicalIF":2.9,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148275171","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Computational Simulations of Biofilm-Associated Proteins Generated by Pathogenic Escherichia coli Identified by MALDI-TOF-TOF Mass Spectrometry and Top-Down Protein Analysis MALDI-TOF-TOF质谱和自上而下蛋白分析鉴定致病性大肠杆菌生物膜相关蛋白的计算模拟

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-08-18 DOI: 10.1021/jasms.6c00188

Mahesh Koirala, Yanlin Shi, Michelle Q. Carter, Clifton K. Fagerquist

{"title":"Computational Simulations of Biofilm-Associated Proteins Generated by Pathogenic Escherichia coli Identified by MALDI-TOF-TOF Mass Spectrometry and Top-Down Protein Analysis","authors":"Mahesh Koirala, Yanlin Shi, Michelle Q. Carter, Clifton K. Fagerquist","doi":"10.1021/jasms.6c00188","DOIUrl":"https://doi.org/10.1021/jasms.6c00188","url":null,"abstract":"Fiveproteins extracted from bacterial biofilms of apathogenic Escherichia coli strainwere identified by MALDI-TOF-TOFmass spectrometry and top-down protein analysis. They are cold-shockproteins CspC and CspE, DNA-binding proteins HU-α and HU-βand CsgA (the major subunit of curli). The fragmentation efficiencyof these singly charged protein ions varied considerably. The patternof fragment ions obtained from tandem mass spectrometry postsourcedecay of these protein ions was compared to in silico protein structures obtained using AlphaFold3 to better understandthe factors that contribute to their gas phase dissociation as wellas their likelihood of unfolding during MALDI sample preparation.Molecular dynamic simulations were performed to calculate the root-mean-squarefluctuations (RMSF) of Cα atoms and root-mean-squaredeviation (RMSD) of the protein backbone to assess their propensityto unfold/denature during MALDI sample preparation. A molecular dynamicssimulation was performed on a curli multimer composed of one CsgB(the minor curli subunit) and five CsgA which showed rapid disintegrationof this short curli complex in hexafluoro-isopropanol (HFIP) consistentwith experimental observations. Strong hydrogen bonding of HFIP appearsto disrupt the intermolecular hydrogen bonds of thisamyloid protein complex but does not unfold CsgA monomer because of138 intramolecular hydrogen bonds present in itssolenoidal β-sheet structure. Finally, electrostatic analysisof the curli complex reveals partitioned regions of positive and negativecharge along the fibril axis that may facilitate its assembly.","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 9","pages":"2155–2167"},"PeriodicalIF":2.9,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148870299","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Triboelectric Nanogenerator-Driven Laser Ablation Electrospray Ionization Enables Neutral Lipid Ionization and in Situ Double-Bond Localization 摩擦电纳米发电机驱动的激光烧蚀电喷雾电离使中性脂质电离和原位双键定位

IF 2.9 2区化学

Journal of the American Society for Mass Spectrometry Pub Date : 2026-09-02 Epub Date: 2026-07-30 DOI: 10.1021/jasms.6c00123

Joseph L. Corstvet, David P. Lewis, Dmitry Leontyev, Xin Ma, Carter K. Asef, Rebecca S. Arnold, John A. Petros, Facundo M. Fernández

{"title":"Triboelectric Nanogenerator-Driven Laser Ablation Electrospray Ionization Enables Neutral Lipid Ionization and in Situ Double-Bond Localization","authors":"Joseph L. Corstvet, David P. Lewis, Dmitry Leontyev, Xin Ma, Carter K. Asef, Rebecca S. Arnold, John A. Petros, Facundo M. Fernández","doi":"10.1021/jasms.6c00123","DOIUrl":"https://doi.org/10.1021/jasms.6c00123","url":null,"abstract":"Ambientionization mass spectrometry includes numerous techniques,many of which are useful for analyzing lipids in biological samples.We report the development of a triboelectric nanogenerator (TENG)-drivenlaser ablation electrospray ionization (LAESI) platform, a novel ambientionization method for the direct analysis of lipid mixtures. Detailedstructural lipid annotation remains challenging due to the structuraldiversity of lipids. Previous research has shown that a TENG-drivendual nanoelectrospray ionization (nESI) and atmospheric pressure chemicalionization (APCI) mechanism helps localize lipid double bonds. Inthis study, we integrated infrared (IR) laser ablation with TENG nESI(TENG-LAESI). This novel ionization platform can ablate and ionizeneutral lipids, including cholesterol and its derivatives, unsaturatedfatty acids, and complex lipid mixtures. Rapid MS analysis revealsdistinct ionization regimes within each TENG pulse and provides temporalresolution for various sterol species. Critically, the APCI stagedrives epoxidation of fatty acid double bonds, generating diagnosticfragmentation patterns that enable reagent-free double-bond positionassignment through tandem MS experiments, without chemical derivatization.Lastly, a novel TENG device was created and compared to existing designs,showing increased epoxidation efficiency and ionization potential.These experiments demonstrate the analytical potential of TENG-LAESIfor structural lipid annotation and establish a foundation for itsfuture development as a spatially resolved ambient MS imaging platform.","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 9","pages":"2085–2093"},"PeriodicalIF":2.9,"publicationDate":"2026-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148870534","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0