ArticleAnalytical chemistry2025
Does Native Capillary Zone Electrophoresis-Mass Spectrometry Maintain the Structural Topology of Protein Complexes?
Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Native CZE-MS analysis of antibodies and hemoglobin using protein-adapted CZE and ESI conditions for detailed proteoform characterization.Analytical and bioanalytical chemistry · 2026Article
- Native Multidimensional Protein Complex Identification and Topology Characterization (Native MudPIT).Analytical chemistry · 2026Article
- Sheath-Liquid CE-MS Interface: A Robust Infusion Platform for Native IMS-MS Analysis of Protein Assemblies and Their Conformers.Journal of mass spectrometry : JMS · 2026Article
- Active peptides pursuit from complicated matrices via tracing ligand-protein complex with MS/MS: Chaperone screening for lysozyme as a pilot study.Journal of pharmaceutical analysis · 2026Article
- Recent Developments and Applications of Capillary and Microchip Electrophoresis in Proteomics and Peptidomics (2023-2025).Journal of separation science · 2026Review
- Decades of dreams coming true: capillary zone electrophoresis-mass spectrometry for reproducible multi-level proteomics.bioRxiv : the preprint server for biology · 2026Article
- Quantitative Native Proteomics by Capillary Zone Electrophoresis-Mass Spectrometry.Analytical chemistry · 2025Article
- Reduced Pressure Ionization Enhances Native Mass Spectrometry of Proteins and Protein Complexes.Angewandte Chemie (International ed. in English) · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
Native capillary zone electrophoresis-mass spectrometry (nCZE-MS) is a useful analytical tool for studying protein complexes. However, the extent to which the protein complexes maintain their native structural topology in nCZE-MS compared to traditional native MS (nMS) is still not fully characterized. In this technical note, we contribute to this topic by coupling nCZE-MS with surface-induced dissociation (SID) for two well-studied protein complexes (streptavidin and human recombinant C-reactive protein). SID cleaves the weakest interface of a given complex, making it a powerful diagnostic tool for identifying perturbations of protein complex structures based on fragmentation patterns. The SID fragmentation patterns of the two protein complexes from nCZE-MS under normal and charge-reducing conditions show a high similarity index compared to those from direct infusion. Additionally, nCZE-MS shows the potential to separate different conformations or different proton distributions that have subtle differences. Although only two cases are shown, the results suggest that nCZE-MS can maintain the native-like structural topology of protein complexes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.