{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T17:09:23Z","timestamp":1788282563549,"version":"build-2803163510"},"reference-count":63,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2026,2,18]],"date-time":"2026-02-18T00:00:00Z","timestamp":1771372800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100005203","name":"OeAD","doi-asserted-by":"crossref","award":["ICM-2016-03196"],"award-info":[{"award-number":["ICM-2016-03196"]}],"id":[{"id":"10.13039\/501100005203","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteomes"],"abstract":"<jats:p>Background: Low-volume trapping columns are essential for sample enrichment, desalting, and injection profile focusing on nano-LC\u2013MS-based proteomics. They enable higher sample loading, improve chromatographic performance, and protect the analytical column by removing salts and contaminants. Recently, monolithic trap columns with micropillar architecture have emerged as alternatives to conventionally packed traps. This study compares the performance of a packed and a micropillar monolithic trap column for the analysis of tryptic peptides. Methods: A tryptic digest of HeLa cell lysate was analyzed under identical LC\u2013MS conditions using both trap types. Peptides were detected at 214 nm and analyzed by nano-ESI on a Q Exactive Plus Orbitrap. Data were searched against the human UniProt database (February 2023) using FragPipe v20.0, and statistical evaluation of MaxLFQ intensities was performed in Perseus using Welch\u2019s t-test and clustering analysis. Results: Over 2500 proteins were identified with both setups. The packed trap column yielded more total peptides, particularly those with post-translational modifications and higher hydrophilicity, whereas the monolithic column favored peptides of intermediate hydrophobicity. Chromatographic profiles confirmed a slight reduction in the trapping efficiency of hydrophilic peptides by the monolithic trap. Conclusions: Trap column design significantly influences peptide recovery and proteome coverage.<\/jats:p>","DOI":"10.3390\/proteomes14010010","type":"journal-article","created":{"date-parts":[[2026,2,18]],"date-time":"2026-02-18T07:50:30Z","timestamp":1771401030000},"page":"10","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Comparison of the Trapping Efficiency for Tryptic Peptides on Particle-Packed and Micro-Pillar Trap Columns for Proteomics Analyses"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9873-1906","authenticated-orcid":false,"given":"Jadranka","family":"Mileti\u0107 Vukajlovi\u0107","sequence":"first","affiliation":[{"name":"Department of Physical Chemistry, Vin\u010da Institute of Nuclear Sciences, National Institute of the Republic of Serbia, University of Belgrade, 11000 Belgrade, Serbia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4271-4370","authenticated-orcid":false,"given":"Bojana","family":"Ili\u0107","sequence":"additional","affiliation":[{"name":"Department of Physical Chemistry, Vin\u010da Institute of Nuclear Sciences, National Institute of the Republic of Serbia, University of Belgrade, 11000 Belgrade, Serbia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5154-4735","authenticated-orcid":false,"given":"Bella","family":"Bruszel","sequence":"additional","affiliation":[{"name":"Institute of Science and Technology, 3400 Klosterneuburg, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6569-4398","authenticated-orcid":false,"given":"Tanja","family":"Pani\u0107-Jankovi\u0107","sequence":"additional","affiliation":[{"name":"Klinik Landstrasse, Zentrallaboratorium mit Blutbank, Juchgasse 25, 1030 Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1964-3965","authenticated-orcid":false,"given":"Goran","family":"Mitulovi\u0107","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine, Medical University of Vienna, 1090 Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,2,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.chroma.2014.06.072","article-title":"Strategies to reduce aspecific adsorption of peptides and proteins in liquid chromatography\u2013mass spectrometry based bioanalyses: An overview","volume":"1358","author":"Maes","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.chroma.2014.07.086","article-title":"Improved sensitivity of the nano ultra-high performance liquid chromatography-tandem mass spectrometric analysis of low-concentrated neuropeptides by reducing aspecific adsorption and optimizing the injection solvent","volume":"1360","author":"Maes","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/j.chroma.2011.12.088","article-title":"Estimation and optimization of the peak capacity of one-dimensional gradient high performance liquid chromatography using a long monolithic silica capillary column","volume":"1228","author":"Horie","year":"2012","journal-title":"J. Chromatogr. A"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1468","DOI":"10.1002\/jssc.200700012","article-title":"Assessing a novel microfluidic interface for shotgun proteome analyses","volume":"30","author":"Staes","year":"2007","journal-title":"J. Sep. Sci."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1093\/bfgp\/ell034","article-title":"HPLC techniques for proteomics analysis\u2014A short overview of latest developments","volume":"5","author":"Mitulovic","year":"2006","journal-title":"Brief. Funct. Genom. Proteomic."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.chroma.2006.01.038","article-title":"Fast, high-efficiency peptide separations on a 50-microm reversed-phase silica monolith in a nanoLC-MS set-up","volume":"1120","author":"Rieux","year":"2006","journal-title":"J. Chromatogr. A"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"4646","DOI":"10.1021\/acs.jproteome.1c00611","article-title":"Multiomics Method Enabled by Sequential Metabolomics and Proteomics for Human Pluripotent Stem-Cell-Derived Cardiomyocytes","volume":"20","author":"Bayne","year":"2021","journal-title":"J. Proteome Res."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"3826","DOI":"10.1021\/pr500530e","article-title":"Off-Line Multidimensional Liquid Chromatography and Auto Sampling Result in Sample Loss in LC\/LC\u2013MS\/MS","volume":"13","author":"Magdeldin","year":"2014","journal-title":"J. Proteome Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.chroma.2014.10.107","article-title":"Enrichment and separation techniques for large-scale proteomics analysis of the protein post-translational modifications","volume":"1372","author":"Huang","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.1021\/pr401026y","article-title":"Empirical multidimensional space for scoring peptide spectrum matches in shotgun proteomics","volume":"13","author":"Ivanov","year":"2014","journal-title":"J. Proteome Res."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1021\/ac2028485","article-title":"Multidimensional Protein Identification Technology-Selected Reaction Monitoring Improving Detection and Quantification for Protein Biomarker Studies","volume":"84","author":"Krisp","year":"2012","journal-title":"Anal. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.chroma.2011.06.038","article-title":"Selective comprehensive multidimensional separation for resolution enhancement in high performance liquid chromatography. Part II: Applications","volume":"1228","author":"Groskreutz","year":"2012","journal-title":"J. Chromatogr. A"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2074","DOI":"10.1002\/rcm.2563","article-title":"Ultra-fast tandem mass spectrometry scanning combined with monolithic column liquid chromatography increases throughput in proteomic analysis","volume":"20","author":"Batycka","year":"2006","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.chroma.2017.03.043","article-title":"Self-packed core shell nano liquid chromatography columns and silica-based monolithic trap columns for targeted proteomics","volume":"1498","author":"Berg","year":"2017","journal-title":"J. Chromatogr. A"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"7579","DOI":"10.1016\/j.chroma.2010.10.037","article-title":"Particle-packed column versus silica-based monolithic column for liquid chromatography-electrospray-linear ion trap-tandem mass spectrometry multiallergen trace analysis in foods","volume":"1217","author":"Bignardi","year":"2010","journal-title":"J. Chromatogr. A"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.1021\/jf4036645","article-title":"Effective and reusable monolith capillary trap of nitrosamine extraction by superheated water from frankfurter sausage","volume":"62","author":"Chienthavorn","year":"2014","journal-title":"J. Agric. Food Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.1002\/elps.200700513","article-title":"Automation of nanoflow liquid chromatography-tandem mass spectrometry for proteome and peptide profiling analysis by using a monolithic analytical capillary column","volume":"29","author":"Jiang","year":"2008","journal-title":"Electrophoresis"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"12452","DOI":"10.1021\/acs.analchem.2c02609","article-title":"Parallelization with Dual-Trap Single-Column Configuration Maximizes Throughput of Proteomic Analysis","volume":"94","author":"Kreimer","year":"2022","journal-title":"Anal. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1021\/ac061603h","article-title":"MicroSPE-nanoLC-ESI-MS\/MS using 10-microm-i.d. silica-based monolithic columns for proteomics","volume":"79","author":"Luo","year":"2007","journal-title":"Anal. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"6151","DOI":"10.1016\/j.chroma.2009.06.072","article-title":"Online capillary weak cation exchange enrichment hyphenated to nanospray mass spectrometry for quantitation of a basic pegvisomant derived peptide","volume":"1216","author":"Neubert","year":"2009","journal-title":"J. Chromatogr. A"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"461097","DOI":"10.1016\/j.chroma.2020.461097","article-title":"Polymeric monolithic microcartridges with gold nanoparticles for the analysis of protein biomarkers by on-line solid-phase extraction capillary electrophoresis-mass spectrometry","volume":"1622","author":"Pont","year":"2020","journal-title":"J. Chromatogr. A"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.chroma.2006.09.072","article-title":"Capillary scale monolithic trap column for desalting and preconcentration of peptides and proteins in one- and two-dimensional separations","volume":"1136","author":"Schley","year":"2006","journal-title":"J. Chromatogr. A"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"462218","DOI":"10.1016\/j.chroma.2021.462218","article-title":"Performance of nanoflow liquid chromatography using core-shell particles: A comparison study","volume":"1648","author":"Liu","year":"2021","journal-title":"J. Chromatogr. A"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"461279","DOI":"10.1016\/j.chroma.2020.461279","article-title":"Separation efficiency kinetics of capillary flow micro-pillar array columns for liquid chromatography","volume":"1626","author":"Desmet","year":"2020","journal-title":"J. Chromatogr. A"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.chroma.2014.09.060","article-title":"Evaluation of the impact of peak description on the quantitative capabilities of comprehensive two-dimensional liquid chromatography","volume":"1368","author":"Place","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.chroma.2012.11.043","article-title":"Study on the performance of different types of three-dimensional chromatographic systems","volume":"1271","author":"Davydova","year":"2013","journal-title":"J. Chromatogr. A"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.chroma.2011.08.003","article-title":"Kinetic plot based comparison of the efficiency and peak capacity of high-performance liquid chromatography columns: Theoretical background and selected examples","volume":"1228","author":"Broeckhoven","year":"2012","journal-title":"J. Chromatogr. A"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.chroma.2012.05.033","article-title":"Peak capacity optimisation for high resolution peptide profiling in complex mixtures by liquid chromatography coupled to time-of-flight mass spectrometry: Application to the Conus consors cone snail venom","volume":"1259","author":"Eugster","year":"2012","journal-title":"J. Chromatogr. A"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.chroma.2014.11.063","article-title":"Nanostructured porous polymer monolithic columns for capillary liquid chromatography of peptides","volume":"1374","author":"Vaast","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"14702","DOI":"10.1021\/acs.analchem.0c03262","article-title":"Improved Sensitivity of Ultralow Flow LC-MS-Based Proteomic Profiling of Limited Samples Using Monolithic Capillary Columns and FAIMS Technology","volume":"92","author":"Kostas","year":"2020","journal-title":"Anal. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.chroma.2014.03.025","article-title":"Band broadening along gradient reversed phase columns: A potential gain in resolution factor","volume":"1342","author":"Gritti","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.chroma.2014.07.020","article-title":"Profiling of drug binding proteins by monolithic affinity chromatography in combination with liquid chromatography\u2013tandem mass spectrometry","volume":"1359","author":"Zhang","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.chroma.2014.07.065","article-title":"Mass transport of small retained molecules in polymer-based monolithic columns","volume":"1362","author":"Gritti","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"6232","DOI":"10.1038\/srep06232","article-title":"Antibody-coupled monolithic silica microtips for highthroughput molecular profiling of circulating exosomes","volume":"4","author":"Ueda","year":"2014","journal-title":"Sci. Rep."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.chroma.2012.10.068","article-title":"Monolithic cryopolymers with embedded nanoparticles. I. Capillary liquid chromatography of proteins using neutral embedded nanoparticles","volume":"1273","author":"Nordborg","year":"2013","journal-title":"J. Chromatogr. A"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.chroma.2013.08.077","article-title":"Monolithic cryopolymers with embedded nanoparticles. II. Capillary liquid chromatography of proteins using charged embedded nanoparticles","volume":"1311","author":"Arrua","year":"2013","journal-title":"J. Chromatogr. A"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.jchromb.2012.11.016","article-title":"Investigation of carryover of peptides in nano-liquid chromatography\/mass spectrometry using packed and monolithic capillary columns","volume":"912","author":"Dolman","year":"2013","journal-title":"J. Chromatogr. B"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/j.chroma.2011.07.014","article-title":"The current revolution in column technology: How it began, where is it going?","volume":"1228","author":"Gritti","year":"2012","journal-title":"J. Chromatogr. A"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.chroma.2012.03.065","article-title":"Hybrid monolithic columns with nanoparticles incorporated for capillary electrochromatography","volume":"1239","author":"Lei","year":"2012","journal-title":"J. Chromatogr. A"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1016\/j.chroma.2010.12.023","article-title":"Kinetic investigation of the relationship between the efficiency of columns and their diameter","volume":"1218","author":"Gritti","year":"2011","journal-title":"J. Chromatogr. A"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"7507","DOI":"10.1016\/j.chroma.2010.09.076","article-title":"Large injection volumes in capillary liquid chromatography: Study of the effect of focusing on chromatographic performance","volume":"1217","year":"2010","journal-title":"J. Chromatogr. A"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1021\/ac9508964","article-title":"Instrumental Requirements for Nanoscale Liquid Chromatography","volume":"68","author":"Chervet","year":"1996","journal-title":"Anal. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1007\/s00216-003-2047-2","article-title":"An improved method for tracking and reducing the void volume in nano HPLC\u2013MS with micro trapping columns","volume":"376","author":"Smoluch","year":"2003","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"5975","DOI":"10.1016\/j.chroma.2010.12.028","article-title":"On-line solid-phase extraction coupled to hydrophilic interaction chromatography-mass spectrometry for the determination of polar drugs","volume":"1218","author":"Fontanals","year":"2011","journal-title":"J. Chromatogr. A"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"7956","DOI":"10.1016\/j.chroma.2011.08.091","article-title":"Rapid and simultaneous determination of hexapeptides (Ac-EEMQRR-amide and H2N-EEMQRR-amide) in anti-wrinkle cosmetics by hydrophilic interaction liquid chromatography\u2013solid phase extraction preparation and hydrophilic interaction liquid chromatography with tandem mass spectrometry","volume":"1218","author":"Zhou","year":"2011","journal-title":"J. Chromatogr. A"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1002\/pmic.200300806","article-title":"Automated, on-line two-dimensional nano liquid chromatography tandem mass spectrometry for rapid analysis of complex protein digests","volume":"4","author":"Mitulovic","year":"2004","journal-title":"Proteomics"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Sch\u00f6binger, M., Klein, O.-J., and Mitulovi\u0107, G. (2016). Low-Temperature Mobile Phase for Peptide Trapping at Elevated Separation Temperature Prior to Nano RP-HPLC-MS\/MS. Separations, 3.","DOI":"10.3390\/chromatography3010006"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.chroma.2019.06.067","article-title":"Pillar array columns for peptide separations in nanoscale reversed-phase chromatography","volume":"1603","year":"2019","journal-title":"J. Chromatogr. A"},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Yu, F., Teo, G.C., Kong, A.T., Li, G.X., Demichev, V., and Nesvizhskii, A.I. (2022). One-stop analysis of DIA proteomics data using MSFragger-DIA and FragPipe computational platform. bioRxiv.","DOI":"10.1101\/2022.10.28.514272"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Desai, H., Ofori, S., Boatner, L., Yu, F., Villanueva, M., Ung, N., Nesvizhskii, A.I., and Backus, K. (2023). Multi-omic stratification of the missense variant cysteinome. bioRxiv.","DOI":"10.1101\/2023.08.12.553095"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Yu, F., Deng, Y., and Nesvizhskii, A.I. (2024). MSFragger-DDA+ Enhances Peptide Identification Sensitivity with Full Isolation Window Search. bioRxiv.","DOI":"10.1101\/2024.10.12.618041"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","article-title":"A simple method for displayng the hydropathic character of a protein","volume":"157","author":"Kyte","year":"1982","journal-title":"J. Mol. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"4","DOI":"10.32614\/RJ-2015-001","article-title":"Peptides: A Package for Data Mining of Antimicrobial Peptides","volume":"7","author":"Osorio","year":"2015","journal-title":"R J."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1038\/nmeth.3901","article-title":"The Perseus computational platform for comprehensive analysis of (prote)omics data","volume":"13","author":"Tyanova","year":"2016","journal-title":"Nat. Methods"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1002\/jssc.201500844","article-title":"Separation of intact proteins on \u03b3-ray-induced polymethacrylate monolithic columns: A highly permeable stationary phase with high peak capacity for capillary high-performance liquid chromatography with high-resolution mass spectrometry","volume":"39","author":"Simone","year":"2016","journal-title":"J. Sep. Sci."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.chroma.2017.03.032","article-title":"A multidimensional liquid chromatography-tandem mass spectrometry platform to improve protein identification in high-throughput shotgun proteomics","volume":"1498","author":"Capriotti","year":"2017","journal-title":"J. Chromatogr. A"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"15311","DOI":"10.1021\/acs.analchem.3c02754","article-title":"Minimize Precolumn Band Broadening with Immiscible Solvent Sandwich Injection","volume":"95","author":"Zhu","year":"2023","journal-title":"Anal. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1983","DOI":"10.1016\/j.chroma.2010.11.086","article-title":"A microfabricated graphitic carbon column for high performance liquid chromatography","volume":"1218","author":"Barrow","year":"2011","journal-title":"J. Chromatogr. A"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1021\/ac203048n","article-title":"Realization of 1 \u00d7 106 theoretical plates in liquid chromatography using very long pillar array columns","volume":"84","author":"Gardeniers","year":"2012","journal-title":"Anal. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"13068","DOI":"10.1021\/acs.analchem.2c02255","article-title":"DirectMS1Quant: Ultrafast Quantitative Proteomics with MS\/MS-Free Mass Spectrometry","volume":"94","author":"Ivanov","year":"2022","journal-title":"Anal. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Szyrwiel, L., Gille, C., M\u00fclleder, M., Demichev, V., and Ralser, M. (2023). Speedy-PASEF: Analytical flow rate chromatography and trapped ion mobility for deep high-throughput proteomics. bioRxiv.","DOI":"10.1101\/2023.02.17.528968"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"e2300100","DOI":"10.1002\/pmic.202300100","article-title":"Fast proteomics with dia-PASEF and analytical flow-rate chromatography","volume":"24","author":"Szyrwiel","year":"2024","journal-title":"Proteomics"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1855","DOI":"10.1038\/s41587-023-02099-7","article-title":"Ultra-fast label-free quantification and comprehensive proteome coverage with narrow-window data-independent acquisition","volume":"42","author":"Guzman","year":"2024","journal-title":"Nat. Biotechnol."}],"container-title":["Proteomes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2227-7382\/14\/1\/10\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,20]],"date-time":"2026-02-20T05:13:36Z","timestamp":1771564416000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2227-7382\/14\/1\/10"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,18]]},"references-count":63,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,3]]}},"alternative-id":["proteomes14010010"],"URL":"https:\/\/doi.org\/10.3390\/proteomes14010010","relation":{},"ISSN":["2227-7382"],"issn-type":[{"value":"2227-7382","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,2,18]]}}}