{"id":{"repo_id":"maryland","oai_identifier":"oai:drum.lib.umd.edu:1903/34583"},"canonical_url":"https://search.dev.ndltd.org/etd/maryland/oai:drum.lib.umd.edu:1903/34583","repository":{"repo_id":"maryland","name":"University of Maryland","base_url":"https://api.drum.lib.umd.edu/server/oai/request"},"display":{"title":"INSTRUMENTAL ADVANCES IN CAPILLARY ELECTROPHORESIS MASS SPECTROMETRY FOR TRACE-SENSITIVE PROTEOMICS","abstract":"Proteomics plays a pivotal role in modern biology by qualitatively and quantitatively characterizing the proteome of biological systems and holistically reflecting the overall dynamics and heterogeneity in organisms. Capillary electrophoresis mass spectrometry (CE-MS) serves as a powerful analytical tool for proteomics and offers superior resolution and minimal sample consumption, yet its adoption has been limited by historical gaps in instrumental development. This dissertation progresses CE-MS proteomics by developing instrumentation and methodologies to promote sensitivity, robustness, scalability, automation, and throughput to facilitate analyses of low-amount proteome samples. The works in this dissertation achieved advances including detection of peptides at sub-picomolar levels (30 zmol), robust analysis of 100 nL proteome samples, and levitational sample enrichment by 4.4 folds. Collectively, this dissertation contributes to the leaping development of CE-MS for proteomics.Chapter 1 overviews the background, current state and challenges of capillary electrophoresis mass spectrometry proteomics and explains research motivation. Chapter 2 introduces methodology combining large-volume sample stacking (LVSS) CE and trapped ion mobility spectrometry (TIMS) for ultra-high-sensitive analysis of low-abundance peptides from mouse brain tissues. Chapter 3 presents a robotic CE-MS system (RoboCap) achieving robust and reproducible analysis of minimal sample volume of proteome. Chapter 4 details an acoustic levitational sample enrichment method for trace-amount proteome. Chapter 5 summarizes the research outcomes in this dissertation and provides potential directions to further improve CE-MS proteomics.","abstract_html":"Proteomics plays a pivotal role in modern biology by qualitatively and quantitatively characterizing the proteome of biological systems and holistically reflecting the overall dynamics and heterogeneity in organisms. Capillary electrophoresis mass spectrometry (CE-MS) serves as a powerful analytical tool for proteomics and offers superior resolution and minimal sample consumption, yet its adoption has been limited by historical gaps in instrumental development. This dissertation progresses CE-MS proteomics by developing instrumentation and methodologies to promote sensitivity, robustness, scalability, automation, and throughput to facilitate analyses of low-amount proteome samples. The works in this dissertation achieved advances including detection of peptides at sub-picomolar levels (30 zmol), robust analysis of 100 nL proteome samples, and levitational sample enrichment by 4.4 folds. Collectively, this dissertation contributes to the leaping development of CE-MS for proteomics.Chapter 1 overviews the background, current state and challenges of capillary electrophoresis mass spectrometry proteomics and explains research motivation. Chapter 2 introduces methodology combining large-volume sample stacking (LVSS) CE and trapped ion mobility spectrometry (TIMS) for ultra-high-sensitive analysis of low-abundance peptides from mouse brain tissues. Chapter 3 presents a robotic CE-MS system (RoboCap) achieving robust and reproducible analysis of minimal sample volume of proteome. Chapter 4 details an acoustic levitational sample enrichment method for trace-amount proteome. Chapter 5 summarizes the research outcomes in this dissertation and provides potential directions to further improve CE-MS proteomics.","abstract_has_math":false,"creators":["Jia, Dashuang"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":"Chemistry","school":null,"contributors":[],"advisors":["Nemes, Peter"],"committee_chairs":[],"committee_members":[],"year":2025,"date_issued":"2025","date_published":"2025","updated_at":"2026-07-24T03:02:06Z","subjects":[],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["https://doi.org/10.13016/qpfq-h2qe"],"render_values":[{"text":"https://doi.org/10.13016/qpfq-h2qe","href":"https://doi.org/10.13016/qpfq-h2qe","code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/1903/34583","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Nemes, Peter"]},{"key":"dc:contributor.department","label":"Department","values":["Chemistry"]},{"key":"dc:creator","label":"Author","values":["Jia, Dashuang"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2025-09-13T05:39:26Z"]},{"key":"dc:date.issued","label":"Date","values":["2025"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://doi.org/10.13016/qpfq-h2qe"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/1903/34583"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Proteomics plays a pivotal role in modern biology by qualitatively and quantitatively characterizing the proteome of biological systems and holistically reflecting the overall dynamics and heterogeneity in organisms. Capillary electrophoresis mass spectrometry (CE-MS) serves as a powerful analytical tool for proteomics and offers superior resolution and minimal sample consumption, yet its adoption has been limited by historical gaps in instrumental development. This dissertation progresses CE-MS proteomics by developing instrumentation and methodologies to promote sensitivity, robustness, scalability, automation, and throughput to facilitate analyses of low-amount proteome samples. The works in this dissertation achieved advances including detection of peptides at sub-picomolar levels (30 zmol), robust analysis of 100 nL proteome samples, and levitational sample enrichment by 4.4 folds. Collectively, this dissertation contributes to the leaping development of CE-MS for proteomics.Chapter 1 overviews the background, current state and challenges of capillary electrophoresis mass spectrometry proteomics and explains research motivation. Chapter 2 introduces methodology combining large-volume sample stacking (LVSS) CE and trapped ion mobility spectrometry (TIMS) for ultra-high-sensitive analysis of low-abundance peptides from mouse brain tissues. Chapter 3 presents a robotic CE-MS system (RoboCap) achieving robust and reproducible analysis of minimal sample volume of proteome. Chapter 4 details an acoustic levitational sample enrichment method for trace-amount proteome. Chapter 5 summarizes the research outcomes in this dissertation and provides potential directions to further improve CE-MS proteomics."]},{"key":"dc:title","label":"Title","values":["INSTRUMENTAL ADVANCES IN CAPILLARY ELECTROPHORESIS MASS SPECTROMETRY FOR TRACE-SENSITIVE PROTEOMICS"]}]}],"canonical_facts":{"dc:contributor.advisor":["Nemes, Peter"],"dc:contributor.department":["Chemistry"],"dc:creator":["Jia, Dashuang"],"dc:date.accessioned":["2025-09-13T05:39:26Z"],"dc:date.issued":["2025"],"dc:description.abstract":["Proteomics plays a pivotal role in modern biology by qualitatively and quantitatively characterizing the proteome of biological systems and holistically reflecting the overall dynamics and heterogeneity in organisms. Capillary electrophoresis mass spectrometry (CE-MS) serves as a powerful analytical tool for proteomics and offers superior resolution and minimal sample consumption, yet its adoption has been limited by historical gaps in instrumental development. This dissertation progresses CE-MS proteomics by developing instrumentation and methodologies to promote sensitivity, robustness, scalability, automation, and throughput to facilitate analyses of low-amount proteome samples. The works in this dissertation achieved advances including detection of peptides at sub-picomolar levels (30 zmol), robust analysis of 100 nL proteome samples, and levitational sample enrichment by 4.4 folds. Collectively, this dissertation contributes to the leaping development of CE-MS for proteomics.Chapter 1 overviews the background, current state and challenges of capillary electrophoresis mass spectrometry proteomics and explains research motivation. Chapter 2 introduces methodology combining large-volume sample stacking (LVSS) CE and trapped ion mobility spectrometry (TIMS) for ultra-high-sensitive analysis of low-abundance peptides from mouse brain tissues. Chapter 3 presents a robotic CE-MS system (RoboCap) achieving robust and reproducible analysis of minimal sample volume of proteome. Chapter 4 details an acoustic levitational sample enrichment method for trace-amount proteome. Chapter 5 summarizes the research outcomes in this dissertation and provides potential directions to further improve CE-MS proteomics."],"dc:identifier":["https://doi.org/10.13016/qpfq-h2qe"],"dc:identifier.uri":["http://hdl.handle.net/1903/34583"],"dc:language.iso":["en"],"dc:title":["INSTRUMENTAL ADVANCES IN CAPILLARY ELECTROPHORESIS MASS SPECTROMETRY FOR TRACE-SENSITIVE PROTEOMICS"],"dc:type":["Dissertation"]},"updated_at":"2026-07-24T03:02:06Z"}