Capillary Electrophoresis-Electrospray Ionization-Mass Spectrometry for Quantitative Analysis of Glycans Labeled with Multiplex Carbonyl-Reactive Tandem Mass Tags
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Recently developed carbonyl-reactive aminoxy tandem mass tag (aminoxyTMT) reagents enable multiplexed characterization and quantitative comparison of structurally complex glycans between different biological samples. Compared to some previously reported isotopic labeling strategies for glycans, the use of the aminoxyTMT method features a simple labeling procedure, excellent labeling efficiency, and reduced spectral complexity at the MS(1) level. Presence of the tertiary amine functionality in the reporter region of the aminoxyTMT labels leads to increased ionization efficiency of the labeled glycans thus improving electrospray ionization (ESI)-mass spectrometry (MS) detection sensitivity. The use of the labeling reagent also makes electrophoretic separation of the labeled neutral and acidic glycans feasible. In this work, we characterized the ESI and collision induced dissociation (CID) behavior of the aminoxyTMT-labeled neutral and sialylated glycans. For the high-mannose N-glycans and small sialylated oligosaccharides, CID fragmentation of [M + Na + H](2+) provides the most informative MS(2) spectra for both quantitative and qualitative analysis. For complex N-glycans, MS(3) of the protonated Y1(H) ion can be used for relative quantification without interference from the HexNAc fragments. Online capillary electrophoresis (CE)-ESI-MS/MS analyses of multiplexed aminoxyTMT-labeled human milk oligosaccharides (HMOs) and different types of N-glycans released from glycoprotein standards were demonstrated. Improved resolution and quantification accuracy of the labeled HMO isomers was achieved by coupling CE with traveling wave ion mobility (TWIM)-CID-MS/MS. N-Glycans released from human serum protein digests were labeled with six-plex aminoxyTMT and subjected to CE-ESI-MS/pseudo-MS(3) analysis, which demonstrated the potential utility of this glycan relative quantification platform for more complex biological samples.
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Quantitative parallel reaction monitoring of peptide abundance had a relative standard deviation of migration time lower than 4% and a relative standard deviation of fragment ion of approximately 20%.
“Sun and co-workers described a quantitative parallel reaction monitoring of peptide abundance where the relative standard deviation (RSD) of the migration time was lower than 4% and the RSD of the fragment ion was approximately 20%132.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [132]
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- Authors
- Zhong, X., Chen, Z., Snovida, S., Liu, Y., Rogers, J. C., & Li, L.
- Affiliations
- University of Wisconsin–Madison (US)
- Thermo Fisher Scientific (United States) (US)
- Xiamen University (CN)
- Corresponding author
- Li, Lingjun
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2015-06-11
- Volume
- 87
- Issue
- 13
- Pages
- 6527-6534
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- PMC
- PMC6314839
- OpenAlex
- W304117529
- Cited by
- 92
- References
- 64
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 10 · 2021: 10 · 2020: 12 · 2019: 9 · 2018: 16 · 2017: 13 · 2016: 11 · 2014: 1
- FWCI
- 5.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Analytical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (NIH R01DK071801, R56DK071801, S10RR029531)
- 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 › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- glycan labeling, N-glycans, sialylated glycans, human milk oligosaccharides, traveling wave ion mobility, collision-induced dissociation, human serum proteins
- MeSH terms
- Polysaccharides, Electrophoresis, Capillary, Spectrometry, Mass, Electrospray Ionization
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