{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T20:27:21Z","timestamp":1783024041328,"version":"3.54.6"},"reference-count":37,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2026,4,21]],"date-time":"2026-04-21T00:00:00Z","timestamp":1776729600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,4,21]],"date-time":"2026-04-21T00:00:00Z","timestamp":1776729600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteomics"],"published-print":{"date-parts":[[2026,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Comprehensive characterization of proteoforms in complex biological systems remains a significant challenge. While native ion\u2010exchange chromatography (IEC) hyphenated with native mass spectrometry (nMS) is a powerful tool for resolving proteoforms, three critical limitations persist: restricted volatile buffers causing nonlinear pH gradients; insufficient coverage of the proteome's broad isoelectric point (pI) range; and inadequate sensitivity for low\u2010abundance proteins. To bridge this gap, we developed an online nanoflow dual IEC\u2010nMS platform. Volatile salt systems for strong anion (SAX) and cation exchange (SCX) were optimized to achieve exceptionally wide and linear pH ranges (2.6\u20135.0 for SAX and 5.0\u20138.5 for SCX). These methods were implemented on self\u2010packed 100\u00a0\u00b5m ID capillary columns at 500 nL\/min to enhance sensitivity. To enable simultaneous analysis of acidic and basic species, we introduced a double\u2010barrel column configuration that integrates nanoSAX and nanoSCX in a noninterfering, parallel manner. This platform was applied to an\n                    <jats:italic>E. coli<\/jats:italic>\n                    cell lysate, identifying 301 unique proteoform masses (D\u2010score &gt; 40) ranging from 10 to 150\u00a0kDa (with about 120&gt; 50\u00a0kDa). Notably, the two modes were highly complementary, with only 10 overlapping species. The double\u2010barrel nanoflow IEC\u2010nMS platform provides a robust, sensitive, and high\u2010resolution strategy for native top\u2010down proteomics, enabling in\u2010depth study of complex proteomes.\n                  <\/jats:p>","DOI":"10.1002\/pmic.70134","type":"journal-article","created":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T05:52:29Z","timestamp":1776837149000},"page":"158-168","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Parallel Analysis of Acidic and Basic Proteoforms in Cell Lysates via Native Cation and Anion Exchange Chromatography\u2014Native Mass Spectrometry"],"prefix":"10.1002","volume":"26","author":[{"given":"Ziran","family":"Zhai","sequence":"first","affiliation":[{"name":"Analytical Chemistry Group and Biocatalysis Group, Van't Hoff Institute For Molecular Sciences (HIMS) University of Amsterdam  Amsterdam The Netherlands"},{"name":"Centre For Analytical Sciences Amsterdam, Van't Hoff Institute For Molecular Sciences (HIMS) University of Amsterdam  Amsterdam The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hafsa","family":"Zakri","sequence":"additional","affiliation":[{"name":"Analytical Chemistry Group and Biocatalysis Group, Van't Hoff Institute For Molecular Sciences (HIMS) University of Amsterdam  Amsterdam The Netherlands"},{"name":"Centre For Analytical Sciences Amsterdam, Van't Hoff Institute For Molecular Sciences (HIMS) University of Amsterdam  Amsterdam The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matteo","family":"Damian","sequence":"additional","affiliation":[{"name":"Analytical Chemistry Group and Biocatalysis Group, Van't Hoff Institute For Molecular Sciences (HIMS) University of Amsterdam  Amsterdam The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesco G.","family":"Mutti","sequence":"additional","affiliation":[{"name":"Analytical Chemistry Group and Biocatalysis Group, Van't Hoff Institute For Molecular Sciences (HIMS) University of Amsterdam  Amsterdam The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Garry","family":"Corthals","sequence":"additional","affiliation":[{"name":"Analytical Chemistry Group and Biocatalysis Group, Van't Hoff Institute For Molecular Sciences (HIMS) University of Amsterdam  Amsterdam The Netherlands"},{"name":"Centre For Analytical Sciences Amsterdam, Van't Hoff Institute For Molecular Sciences (HIMS) University of Amsterdam  Amsterdam The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea F. 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