Coupling porous sheathless interface MS with transient‐ITP in neutral capillaries for improved sensitivity in glycopeptide analysis
Abstract
I g G antibodies are modulated in their function by the specific structure of the N‐glycans attached to their F c (fragment crystallizable) portions. However, the glycosylation analysis of antigen‐specific I g G s is a challenging task as antibody levels to a given antigen only represent a fraction of the total I g G levels. Here, we investigated the use of a transient‐ITP (t‐ITP)—MS method for highly sensitive I g G 1 glycosylation profiling as a complementary method to a high‐throughput nano‐RPLC‐MS method. It was found that t‐ITP‐CZE using neutrally coated separation capillaries with a large volume injection (37% of capillary volume) and interfaced to MS with a sheathless porous sprayer yielded a 40‐fold increase in sensitivity for I g G 1 F c glycopeptide analysis when compared to the conventional strategy. Furthermore, the glycoform profiles found with the t‐ITP‐CZE strategy were comparable to those from nano‐RPLC‐MS. In conclusion, the use of the highly sensitive t‐ITP‐CZE‐MS method will provide information on I g G F c glycosylation for those samples with IgG1 concentrations below the LOD s of the conventional method.
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tITP requires optimization of both electrolyte concentrations and loading volume for efficient stacking of target analytes.
“tITP requires an optimization of both electrolyte concentrations and loading volume to enable efficient stacking of the target analytes13,27,65,120–122.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [122]
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“reported the use of a similar methodology for highly sensitive IgG1 glycosylation profiling as a complementary method to a highthroughput nano-RPLC-MS [29].”
MethodCapillary zone electrophoresis-mass spectrometry for bottom-up proteomics
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“This high level of reproducibility is in line with previously published quantitative results obtained when analyzing single peptides [37,38].”
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Wang, C. (2014) · University Libraries (University of Maryland)
- Authors
- Heemskerk, A. A. M., Wuhrer, M., Busnel, J., Koeleman, C. A. M., Selman, M. H. J., Vidarsson, G., Kapur, R., Schoenmaker, B., Derks, R. J. E., Deelder, A. M., & Mayboroda, O. A.
- Affiliations
- Leiden University Medical Center (NL)
- Sanquin (NL)
- Corresponding author
- Heemskerk, Anthonius A. M.
- ORCID
- Venue
- ELECTROPHORESIS
- Publisher
- Wiley
- Published
- 2013-01-03
- Volume
- 34
- Issue
- 3
- Pages
- 383-387
- ISSN
- 0173-0835 (ISSN-L)
- 1522-2683
- OpenAlex
- W2019249724
- Cited by
- 43
- References
- 26
- Citations by year
- 2022: 3 · 2021: 2 · 2020: 3 · 2019: 6 · 2018: 3 · 2017: 3 · 2016: 5 · 2015: 3 · 2014: 8 · 2013: 6 · 2012: 1
- FWCI
- 3.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Electrophoresis (publishedVersion)
- PubMed (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Leiden Repository (Leiden University) (submittedVersion)
- Pure Amsterdam UMC (submittedVersion)
- Topics
- Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- capillary zone electrophoresis, N-glycan profiling, glycopeptide analysis, large volume injection, antibody glycosylation, detection sensitivity
- MeSH terms
- Glycopeptides, Humans, Immunoglobulin G, Immunoglobulin Fc Fragments, Sensitivity and Specificity, Electrophoresis, Capillary, Spectrometry, Mass, Electrospray Ionization
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