{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T15:05:04Z","timestamp":1791385504143,"version":"4.3.3"},"reference-count":23,"publisher":"American Chemical Society (ACS)","issue":"10","license":[{"start":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T00:00:00Z","timestamp":1788134400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T00:00:00Z","timestamp":1788134400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T00:00:00Z","timestamp":1788134400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35 GM156406"],"award-info":[{"award-number":["R35 GM156406"]}],"id":[{"id":"10.13039\/100000002","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>High-Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) enhances peptide identification in LC-MS proteomics, but whether optimal compensation voltages (CVs) are transferable between mass spectrometry platforms remains unclear. To address this gap, we used the Pierce Peptide Retention Time Calibration (PRTC) mixture comprised of 15 synthetic peptides and analyzed the CV transmission profiles across a wide voltage range (\u221285 to \u221225 V). We systematically evaluated FAIMS CV profiles across three modern Orbitrap mass spectrometers (Astral, Ascend, and Exploris 480), each equipped with different ionization sources and chromatographic systems. Across the three platforms, optimal CVs were conserved within a narrow tolerance (typically \u22645 V), supporting CV portability for routine method transfer under the conditions evaluated. Additionally, we observed that interplatform CV variability was greatest for peptides with strongly negative optimal CVs, consistent with the greater conformational sensitivity of higher charge-density ions under high-field FAIMS conditions. Together, these results suggest that FAIMS CV requirements are predominantly peptide-intrinsic properties under typical bottom-up proteomics conditions and support the use of the PRTC mixture as a practical standard for routine FAIMS calibration and cross-platform quality control in proteomics laboratories.<\/jats:p>","DOI":"10.1021\/jasms.6c00307","type":"journal-article","created":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T05:13:11Z","timestamp":1788412391000},"page":"2577-2584","source":"Crossref","is-referenced-by-count":0,"title":["Cross-Platform Consistency\nof FAIMS Compensation Voltage\nOptimization in Modern Orbitrap Mass Spectrometers"],"prefix":"10.1021","volume":"37","author":[{"given":"Siwen","family":"Zhang","sequence":"first","affiliation":[{"name":"Harvard Medical School , , , ,","place":["Boston, Massachusetts, United States, 02115"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4291-413X","authenticated-orcid":true,"given":"Joao A.","family":"Paulo","sequence":"additional","affiliation":[{"name":"Harvard Medical School , , , ,","place":["Boston, Massachusetts, United States, 02115"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,31]]},"reference":[{"issue":"4","key":"2026100710070020200_cit1","doi-asserted-by":"publisher","first-page":"716","DOI":"10.1074\/mcp.TIR119.001906","article-title":"A Compact\nQuadrupole-Orbitrap Mass Spectrometer with FAIMS Interface Improves\nProteome Coverage in Short LC Gradients","volume":"19","author":"Bekker-Jensen","year":"2020","journal-title":"Mol.\nCell. Proteomics"},{"issue":"15","key":"2026100710070020200_cit2","doi-asserted-by":"publisher","first-page":"9529","DOI":"10.1021\/acs.analchem.8b02233","article-title":"Comprehensive Single-Shot\nProteomics with FAIMS on a Hybrid Orbitrap Mass Spectrometer","volume":"90","author":"Hebert","year":"2018","journal-title":"Anal. Chem"},{"issue":"10","key":"2026100710070020200_cit3","doi-asserted-by":"publisher","first-page":"2051","DOI":"10.1074\/mcp.TIR118.000862","article-title":"A Novel Differential\nIon Mobility Device Expands the Depth of Proteome Coverage and the\nSensitivity of Multiplex Proteomic Measurements","volume":"17","author":"Pfammatter","year":"2018","journal-title":"Mol. Cell. 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Proteome\nRes"},{"issue":"6","key":"2026100710070020200_cit7","doi-asserted-by":"publisher","first-page":"4010","DOI":"10.1021\/acs.analchem.8b05399","article-title":"Characterization\nand Optimization of Multiplexed Quantitative Analyses Using High-Field\nAsymmetric-Waveform Ion Mobility Mass Spectrometry","volume":"91","author":"Schweppe","year":"2019","journal-title":"Anal. Chem"},{"issue":"24","key":"2026100710070020200_cit8","doi-asserted-by":"publisher","first-page":"15959","DOI":"10.1021\/acs.analchem.0c03415","article-title":"Global Phosphoproteome Analysis Using\nHigh-Field Asymmetric\nWaveform Ion Mobility Spectrometry on a Hybrid Orbitrap Mass Spectrometer","volume":"92","author":"Muehlbauer","year":"2020","journal-title":"Anal. Chem"},{"issue":"25","key":"2026100710070020200_cit9","doi-asserted-by":"publisher","first-page":"8704","DOI":"10.1021\/acs.analchem.1c00990","article-title":"Ultrasensitive\nNanoLC-MS of Subnanogram Protein Samples Using Second Generation Micropillar\nArray LC Technology with Orbitrap Exploris 480 and FAIMS PRO","volume":"93","author":"Stejskal","year":"2021","journal-title":"Anal. Chem"},{"issue":"24","key":"2026100710070020200_cit10","doi-asserted-by":"publisher","first-page":"9689","DOI":"10.1021\/ac8016295","article-title":"Fundamentals of\ntraveling wave ion mobility spectrometry","volume":"80","author":"Shvartsburg","year":"2008","journal-title":"Anal.\nChem"},{"key":"2026100710070020200_cit11","doi-asserted-by":"publisher","first-page":"1282","DOI":"10.1016\/S1044-0305(02)00527-5","article-title":"Application of ESI-FAIMS-MS\nto the analysis of tryptic peptides","volume":"13","author":"Barnett","year":"2002","journal-title":"J. Am.\nSoc. Mass Spectrom"},{"key":"2026100710070020200_cit12","doi-asserted-by":"publisher","first-page":"15939","DOI":"10.1021\/acs.analchem.2c01287","article-title":"High-Field\nAsymmetric Waveform Ion Mobility Spectrometry Interface Enhances Parallel\nReaction Monitoring on an Orbitrap Mass Spectrometer","volume":"94","author":"Deng","year":"2022","journal-title":"Anal. Chem"},{"key":"2026100710070020200_cit13","doi-asserted-by":"publisher","first-page":"2453","DOI":"10.1021\/acs.jproteome.2c00337","article-title":"Coupling High-Field\nAsymmetric Ion\nMobility Spectrometry with Capillary Electrophoresis-Electrospray\nIonization-Tandem Mass Spectrometry Improves Protein Identifications\nin Bottom-Up Proteomic Analysis of Low Nanogram Samples","volume":"21","author":"Johnson","year":"2022","journal-title":"J. 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Proteome Res"},{"issue":"8","key":"2026100710070020200_cit16","doi-asserted-by":"publisher","first-page":"1111","DOI":"10.1002\/pmic.201100463","article-title":"Using iRT, a normalized\nretention time for more targeted measurement of peptides","volume":"12","author":"Escher","year":"2012","journal-title":"Proteomics"},{"issue":"2","key":"2026100710070020200_cit17","doi-asserted-by":"publisher","first-page":"1138","DOI":"10.1021\/pr900816a","article-title":"Comparison of Database\nSearch Strategies for High Precursor Mass Accuracy MS\/MS Data","volume":"9","author":"Hsieh","year":"2010","journal-title":"J. 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Chim.\nActa"},{"issue":"1","key":"2026100710070020200_cit23","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","article-title":"A simple method for displaying the hydropathic character\nof a protein","volume":"157","author":"Kyte","year":"1982","journal-title":"J Mol Biol"}],"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.6c00307","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jamsef\/article-pdf\/37\/10\/2577\/68025351\/jasms.6c00307.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jamsef\/article-pdf\/37\/10\/2577\/68025351\/jasms.6c00307.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T14:43:11Z","timestamp":1791384191000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jamsef\/article\/37\/10\/2577\/5388134\/Cross-Platform-Consistency-of-FAIMS-Compensation"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,31]]},"references-count":23,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2026,8,31]]},"published-print":{"date-parts":[[2026,10,7]]}},"URL":"https:\/\/doi.org\/10.1021\/jasms.6c00307","relation":{},"ISSN":["1044-0305","1879-1123"],"issn-type":[{"value":"1044-0305","type":"print"},{"value":"1879-1123","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,31]]}}}