Capillary zone electrophoresis coupled to drift tube ion mobility-mass spectrometry for the analysis of native and APTS-labeled N-glycans
Abstract
Capillary zone electrophoresis (CZE) based on electrophoretic mobility in the liquid phase and ion mobility spectrometry (IMS) based on mobilities in the gas phase are both powerful techniques for the separation of complex samples. Protein glycosylation is one of the most common post-translational modifications associated with a wide range of biological functions and human diseases. Due to their high structural variability, the analysis of glycans still represents a challenging task. In this work, the first on-line coupling of CZE with drift tube ion mobility-mass spectrometry (DTIM-MS) has been perfomed to further improve separation capabilities for the analysis of native and 8-aminopyrene-1,3,6-trisulfonic acid (APTS)-labeled N-glycans. In this way, a complexity of glycan signals was revealed which could not be resolved by these techniques individually, shown for both native and APTS-labeled glycans. Each individual glycan signal separated in CZE exhibited an unexpectedly high number of peaks observed in the IMS dimension. This observation could potentially be explained by the presence of isomeric forms, including different linkages, and/or gas-phase conformers. In addition, the type of sialic acid attached to glycans has a significant impact on the obtained drift time profile. Furthermore, the application of α2-3 neuraminidase enabled the partial assignment of peaks in the arrival time distribution considering their sialic acid linkages (α2-3/α2-6). This work is a showcase for the high potential of CZE-DTIM-MS, which is expected to find various applications in the future. Graphical abstract ᅟ.
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Jooss et al. showed the first successful application of CZE with drift tube ion mobility-mass spectrometry for separation and characterization of native and APTS-labeled N-glycans released from different protein sources.
“In another report, Jooss et al. showed, for the first time, a successful application of CZE in conjunction with drift tube ion mobility-mass spectrometry (DTIM-MS) for the separation and characterization of native and APTS-labeled N-glycans released from different protein sources90.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [90]
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Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research
Gomes, F. P., & Yates, J. R. (2019) · Mass Spectrometry Reviews · doi:10.1002/mas.21599 · Cited by 112 · see citing works
- Authors
- Jooß, K., Meckelmann, S. W., Klein, J., Schmitz, O. J., & Neusüß, C.
- Affiliations
- Helmholtz Munich (DE)
- University of Duisburg-Essen (DE)
- Hochschule Aalen (DE)
- Corresponding author
- Neusüß, Christian
- Venue
- Analytical and Bioanalytical Chemistry
- Published
- 2018-12-10
- Volume
- 411
- Issue
- 24
- Pages
- 6255-6264
- ISSN
- 1618-2642 (ISSN-L)
- 1618-2650
- OpenAlex
- W2904553140
- Cited by
- 41
- References
- 0
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 9 · 2021: 9 · 2020: 4 · 2019: 8 · 2017: 1
- FWCI
- 1.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Analytical and Bioanalytical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- OPUS (Aalen University) (submittedVersion)
- Site cant be reached (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
- Keywords
- capillary zone electrophoresis, N-glycans, protein glycosylation, sialic acid, glycan isomers, gas-phase conformers, on-line coupling
- MeSH terms
- Ion Mobility Spectrometry, Antibodies, Monoclonal, Glycosylation, Polysaccharides, Pyrenes, Electrophoresis, Capillary, Spectrometry, Mass, Electrospray Ionization
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