ArticleAnalytical chemistry2024
Direct and Detailed Site-Specific Glycopeptide Characterization by Higher-Energy Electron-Activated Dissociation Tandem Mass Spectrometry.
Article in Analytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Navigating the glycomics landscape with CE-MS: advances in sample preparation and analytical strategies.The Analyst · 2026Review
- Evaluating the Performance of Photon- and Electron-Based Fragmentation Methods in Omnitrap-LCMS Analysis ofAnalytical chemistry · 2026Article
- Enhancing ginsenoside isomers annotation by integrated analysis of electron-activated dissociation and collision-induced dissociation tandem mass spectrometry.Journal of pharmaceutical analysis · 2026Article
- Optimization of LC-ExD methods for glycopeptides on an Omnitrap-Orbitrap platform.Analytical and bioanalytical chemistry · 2026Article
- Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026Review
- Mass Spectrometry Analysis of Biotherapeutic Monoclonal Antibody Glycosylation.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Recent Advances in Mass Spectrometry-Based Bottom-Up Proteomics.Analytical chemistry · 2025Review
- Autonomous Dissociation-type Selection for Glycoproteomics Using a Real-Time Library Search.Journal of proteome research · 2024Article
- External Data Systems Enable Enhanced (and Sustainable) Fourier Transform Mass Spectrometry Imaging for Legacy Hybrid Linear Ion Trap-Orbitrap Platforms.Journal of the American Society for Mass Spectrometry · 2024Article
- Glycoproteomics: Charting new territory in mass spectrometry and glycobiology.Journal of mass spectrometry : JMS · 2024Review
- First 20 Years of Orbitrap Mass Spectrometry as the Mainstream Analytical Technique.Mass spectrometry reviewsReview
- Software Design and Analytical Challenges for Confident Glycopeptide Identification With Data-Independent Acquisition.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
Glycosylation is widely recognized as the most complex post-translational modification due to the widespread presence of macro- and microheterogeneities, wherein its biological consequence is closely related to both the glycosylation sites and the glycan fine structures. Yet, efficient site-specific detailed glycan characterization remains a significant analytical challenge. Here, utilizing an Orbitrap-Omnitrap platform, higher-energy electron-activated dissociation (heExD) tandem mass spectrometry (MS/MS) revealed extraordinary efficacy for the structural characterization of intact glycopeptides. HeExD produced extensive fragmentation within both the glycan and the peptide, including A-/B-/C-/Y-/Z-/X-ions from the glycan motif and a-/b-/c-/x-/y-/z-type peptide fragments (with or without the glycan). The intensity of cross-ring cleavage and backbone fragments retaining the intact glycan was highly dependent on the electron energy. Among the four electron energy levels investigated, electronic excitation dissociation (EED) provided the most comprehensive structural information, yielding a complete series of glycosidic fragments for accurate glycan topology determination, a wealth of cross-ring fragments for linkage definition, and the most extensive peptide backbone fragments for accurate peptide sequencing and glycosylation site localization. The glycan fragments observed in the EED spectrum correlated well with the fragmentation patterns observed in EED MS/MS of the released glycans. The advantages of EED over higher-energy collisional dissociation (HCD), stepped collision energy HCD (sceHCD), and electron-transfer/higher-energy collisional dissociation (EThcD) were demonstrated for the characterization of a glycopeptide bearing a biantennary disialylated glycan. EED can produce a complete peptide backbone and glycan sequence coverage even for doubly protonated precursors. The exceptional performance of heExD MS/MS, particularly EED MS/MS, in site-specific detailed glycan characterization on an Orbitrap-Omnitrap hybrid instrument presents a novel option for in-depth glycosylation analysis.
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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.