{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T14:58:26Z","timestamp":1791385106183,"version":"4.3.3"},"reference-count":34,"publisher":"American Chemical Society (ACS)","issue":"10","license":[{"start":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T00:00:00Z","timestamp":1790553600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000153","name":"Division of Biological Infrastructure","doi-asserted-by":"publisher","award":["1951447"],"award-info":[{"award-number":["1951447"]}],"id":[{"id":"10.13039\/100000153","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000165","name":"Division of Chemistry","doi-asserted-by":"publisher","award":["1709526"],"award-info":[{"award-number":["1709526"]}],"id":[{"id":"10.13039\/100000165","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,7]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>A pulsed 193 nm deep ultraviolet (DUV) laser was used to ablate proteins and a noncovalently bound protein assembly deposited on surfaces. DUV laser ablation has been used for ablation of proteins from surfaces without fragmentation; however, DUV ablation of native proteins from surfaces without the loss of higher-order structure of proteins has not been demonstrated. Here, protein charge state distribution (CSD) and collision-induced unfolding (CIU) were used to probe the structure of DUV laser-ablated native proteins. Standard solutions containing native bovine serum albumin (BSA), jack-bean concanavalin A (ConA), and bovine carbonic anhydrase (CA) were deposited on a quartz microscope slide, laser-ablated, and captured for ion mobility-mass spectrometry (IM-MS) analysis. Observed CSD from native MS of conventionally extracted and DUV laser-ablated proteins were comparable. CIU plots for all charge states of laser-ablated proteins exhibited the same ion mobility features and comparable transition voltages (CIU50) as the extracted samples. These results suggest that DUV laser ablation can yield intact proteins with conserved higher-order structures.<\/jats:p>","DOI":"10.1021\/jasms.6c00185","type":"journal-article","created":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T15:01:42Z","timestamp":1790607702000},"page":"2388-2395","source":"Crossref","is-referenced-by-count":0,"title":["Deep Ultraviolet Laser\nAblation Surface Sampling for\nNative Mass Spectrometry"],"prefix":"10.1021","volume":"37","author":[{"ORCID":"https:\/\/orcid.org\/0009-0001-9810-9439","authenticated-orcid":true,"given":"Neda","family":"Feizi","sequence":"first","affiliation":[{"name":"Baylor University , , , ,","place":["Waco, Texas, United States, 76798"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3173-937X","authenticated-orcid":true,"given":"Kadeem O.","family":"Hayes","sequence":"additional","affiliation":[{"name":"Louisiana State University , , , ,","place":["Baton Rouge, Louisiana, United States, 70803"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kelcey B.","family":"Hines","sequence":"additional","affiliation":[{"name":"Louisiana State University , , , ,","place":["Baton Rouge, Louisiana, United States, 70803"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raul A.","family":"Villacob","sequence":"additional","affiliation":[{"name":"Baylor College of Medicine , , , ,","place":["Houston, Texas, United States, 77030"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4976-2263","authenticated-orcid":true,"given":"Kermit K.","family":"Murray","sequence":"additional","affiliation":[{"name":"Louisiana State University , , , ,","place":["Baton Rouge, Louisiana, United States, 70803"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4209-9200","authenticated-orcid":true,"given":"Touradj","family":"Solouki","sequence":"additional","affiliation":[{"name":"Baylor University , , , ,","place":["Waco, Texas, United States, 76798"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,28]]},"reference":[{"issue":"12","key":"2026100710065223500_cit1","doi-asserted-by":"publisher","first-page":"2531","DOI":"10.1021\/jasms.0c00226","article-title":"Native Mass Spectrometry Imaging and in Situ Top-down\nIdentification of Intact Proteins Directly from Tissue","volume":"31","author":"Hale","year":"2020","journal-title":"J. Am. Soc. Mass Spectrom."},{"issue":"5","key":"2026100710065223500_cit2","doi-asserted-by":"publisher","first-page":"2120","DOI":"10.1021\/jacs.1c10032","article-title":"Native Ambient Mass\nSpectrometry Imaging of Ligand-Bound and Metal-Bound Proteins in Rat\nBrain","volume":"144","author":"Sisley","year":"2022","journal-title":"J. Am. Chem. Soc."},{"issue":"1","key":"2026100710065223500_cit3","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1038\/s41596-025-01188-y","article-title":"High-Spatial-Resolution\nMass Spectrometry Imaging of Biological Tissues Using a Microfluidic\nProbe","volume":"21","author":"Jiang","year":"2026","journal-title":"Nat. Protoc."},{"issue":"3","key":"2026100710065223500_cit4","doi-asserted-by":"publisher","first-page":"3185","DOI":"10.1021\/jacs.5c16821","article-title":"Integrated Native\nMass Spectrometry Imaging of Soluble\nand Membrane Proteins","volume":"148","author":"Hale","year":"2026","journal-title":"J. Am. Chem. Soc."},{"issue":"5695","key":"2026100710065223500_cit5","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1126\/science.1104404","article-title":"Mass Spectrometry\nSampling under Ambient Conditions with Desorption Electrospray Ionization","volume":"306","author":"Taka\u0301ts","year":"2004","journal-title":"Science"},{"issue":"4","key":"2026100710065223500_cit6","doi-asserted-by":"publisher","first-page":"873","DOI":"10.1021\/jasms.9b00122","article-title":"Native\nLESA TWIMS-MSI: Spatial, Conformational, and Mass Analysis of Proteins\nand Protein Complexes","volume":"31","author":"Hale","year":"2020","journal-title":"J. Am. Soc. Mass Spectrom."},{"issue":"7","key":"2026100710065223500_cit7","doi-asserted-by":"publisher","first-page":"1179","DOI":"10.1007\/s13361-019-02178-7","article-title":"Cryo-LESA Mass Spectrometry\u2500a\nStep Towards Truly Native Surface Sampling of Proteins","volume":"30","author":"Yan","year":"2019","journal-title":"J. Am. Soc. Mass Spectrom."},{"issue":"19","key":"2026100710065223500_cit8","doi-asserted-by":"publisher","first-page":"12246","DOI":"10.1021\/acs.analchem.9b02075","article-title":"Probing the Fundamentals\nof Native Liquid Extraction\nSurface Analysis Mass Spectrometry of Proteins: Can Proteins Refold\nduring Extraction?","volume":"91","author":"Illes-Toth","year":"2019","journal-title":"Anal. Chem."},{"issue":"7","key":"2026100710065223500_cit9","doi-asserted-by":"publisher","first-page":"4422","DOI":"10.1021\/acs.analchem.7b04306","article-title":"Soft Picosecond\nInfrared Laser Extraction of Highly Charged Proteins and Peptides\nfrom Bulk Liquid Water for Mass Spectrometry","volume":"90","author":"Lu","year":"2018","journal-title":"Anal. Chem."},{"issue":"1","key":"2026100710065223500_cit10","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1007\/s13361-018-2061-4","article-title":"LILBID and nESI: Different\nNative Mass Spectrometry Techniques as Tools in Structural Biology","volume":"30","author":"Peetz","year":"2019","journal-title":"J. Am. Soc. Mass Spectrom."},{"issue":"10","key":"2026100710065223500_cit11","doi-asserted-by":"publisher","first-page":"1981","DOI":"10.1007\/s13361-018-2015-x","article-title":"Liquid Native\nMALDI Mass Spectrometry for the Detection of Protein-Protein Complexes","volume":"29","author":"Beaufour","year":"2018","journal-title":"J. Am. Soc. Mass Spectrom."},{"issue":"3","key":"2026100710065223500_cit12","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1007\/s13361-016-1576-9","article-title":"Isolating\nProtein Charge State Reduction in Electrospray Droplets Using Femtosecond\nLaser Vaporization","volume":"28","author":"Karki","year":"2017","journal-title":"J. Am. Soc. Mass Spectrom."},{"issue":"3","key":"2026100710065223500_cit13","doi-asserted-by":"publisher","first-page":"775","DOI":"10.1007\/s00216-025-06229-9","article-title":"Native Mass Spectrometry Enabled\nby Infrared Matrix-Assisted Laser Desorption Electrospray Ionization\nfor Rapid Measurement of Protein-Ligand Biophysical Parameters","volume":"418","author":"Adepoju","year":"2026","journal-title":"Anal. Bioanal. Chem."},{"issue":"8","key":"2026100710065223500_cit14","doi-asserted-by":"publisher","first-page":"1913","DOI":"10.1021\/jasms.4c00199","article-title":"Detection of Noncovalent Protein\u2013Ligand\nComplexes by IR-MALDESI-MS","volume":"35","author":"Knizner","year":"2024","journal-title":"J. Am. Soc. 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In  Deep Ultraviolet and\nInfrared Laser Ablation of Carbonic Anhydrase Ii; Proceedings\nof the 72nd Conference on Mass Spectrometry\nand Allied Topics 2024."},{"issue":"15","key":"2026100710065223500_cit18","doi-asserted-by":"publisher","first-page":"5723","DOI":"10.1039\/D3SC04933G","article-title":"Laser Capture Microdissection\nand Native Mass Spectrometry for Spatially-Resolved Analysis of Intact\nProtein Assemblies in Tissue","volume":"15","author":"Hughes","year":"2024","journal-title":"Chem. Sci."},{"key":"2026100710065223500_cit19","doi-asserted-by":"publisher","DOI":"10.1016\/j.aca.2021.339021","article-title":"Deep-Ultraviolet\nLaser Ablation Sampling\nfor Proteomic Analysis of Tissue","volume":"1184","author":"Lawal","year":"2021","journal-title":"Anal. 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Protein Stability Differences in Biochemically\nRelevant Salt Solutions","volume":"96","author":"Lee","year":"2024","journal-title":"Anal. Chem."},{"issue":"6","key":"2026100710065223500_cit28","doi-asserted-by":"publisher","first-page":"1929","DOI":"10.1039\/D3AN02070C","article-title":"Native Mass Spectrometry\nAnalysis of Conjugated HSA and BSA Complexes with Various Flavonoids","volume":"149","author":"Alexander","year":"2024","journal-title":"Analyst"},{"issue":"21","key":"2026100710065223500_cit29","doi-asserted-by":"publisher","first-page":"10692","DOI":"10.1021\/ac502590h","article-title":"Characterization\nof Small Protein Aggregates and Oligomers Using Size Exclusion Chromatography\nwith Online Detection by Native Electrospray Ionization Mass Spectrometry","volume":"86","author":"Muneeruddin","year":"2014","journal-title":"Anal. Chem."},{"key":"2026100710065223500_cit30","doi-asserted-by":"publisher","first-page":"22636","DOI":"10.1021\/acs.analchem.5c07180","article-title":"Are Native Conformations\nof Proteins Retained Throughout\nLaser Ablation Capture?","volume":"98","author":"Feizi","year":"2026","journal-title":"Anal. Chem."},{"issue":"11","key":"2026100710065223500_cit31","doi-asserted-by":"publisher","first-page":"3076","DOI":"10.1021\/bi00514a014","article-title":"Thermodynamics of\nConcanavalin a Dimer-Tetramer Self-Association:\nSedimentation Equilibrium Studies","volume":"20","author":"Senear","year":"1981","journal-title":"Biochemistry"},{"issue":"4","key":"2026100710065223500_cit32","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1039\/a907957b","article-title":"Binding of Selected Carbohydrates\nto Apo Concanavalin A Studied by Electrospray Ionization Mass Spectrometry","volume":"125","author":"van Dongen","year":"2000","journal-title":"Analyst"},{"issue":"8","key":"2026100710065223500_cit33","doi-asserted-by":"publisher","first-page":"1272","DOI":"10.1002\/pro.2699","article-title":"Collisional Unfolding of Multiprotein Complexes Reveals\nCooperative Stabilization Upon Ligand Binding","volume":"24","author":"Niu","year":"2015","journal-title":"Protein Sci."},{"issue":"24","key":"2026100710065223500_cit34","doi-asserted-by":"publisher","first-page":"9251","DOI":"10.1021\/ac201576e","article-title":"Quantifying Protein\u2013Protein\nInteractions within Noncovalent Complexes Using Electrospray Ionization\nMass Spectrometry","volume":"83","author":"Erba","year":"2011","journal-title":"Anal. Chem."}],"container-title":["Journal of the American\nSociety for Mass Spectrometry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jasms.6c00185","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jamsef\/article-pdf\/37\/10\/2388\/68678842\/jasms.6c00185.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jamsef\/article-pdf\/37\/10\/2388\/68678842\/jasms.6c00185.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T14:25:03Z","timestamp":1791383103000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jamsef\/article\/37\/10\/2388\/5440107\/Deep-Ultraviolet-Laser-Ablation-Surface-Sampling"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,28]]},"references-count":34,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2026,9,28]]},"published-print":{"date-parts":[[2026,10,7]]}},"URL":"https:\/\/doi.org\/10.1021\/jasms.6c00185","relation":{},"ISSN":["1044-0305","1879-1123"],"issn-type":[{"value":"1044-0305","type":"print"},{"value":"1879-1123","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,28]]}}}