ArticleJournal of the American Society for Mass Spectrometry2018
Identification of Sialic Acid Linkages on Intact Glycopeptides via Differential Chemical Modification Using IntactGIG-HILIC.
Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Protein glycosylation profiling in lung adenocarcinoma and precursor lesions: analysis of FFPE tissue sections.Analytical and bioanalytical chemistry · 2026Article
- Mass Spectrometry-Based Comparative Analysis ofACS chemical neuroscience · 2025Article
- Glycoproteomics analysis of colorectal cancer reveals differential alterations of glycoproteins and glycans.Analytical and bioanalytical chemistry · 2025Article
- Deciphering disease-specific glycosylation: unraveling diabetes subtypes through serum glycopattern.Analytical and bioanalytical chemistry · 2025Article
- Quantitative proteomic and glycoproteomic analysis identifies CLCA1, FBN1, and FGB as potential biomarkers for ulcerative colitis.RSC advances · 2025Article
- Immunoglobulin G Subclass-Specific Glycosylation Changes in Rheumatoid Arthritis.International journal of molecular sciences · 2025Article
- Mass spectrometry analysis of intact proteinJournal of Zhejiang University. Science. B · 2024Article
- Review
- The Hitchhiker's guide to glycoproteomics.Biochemical Society transactions · 2021Review
- Impact of Expressing Cells on Glycosylation and Glycan of the SARS-CoV-2 Spike Glycoprotein.ACS omega · 2021Article
- The structure and role of lactone intermediates in linkage-specific sialic acid derivatization reactions.Glycoconjugate journal · 2021Article
- Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021Review
- Isomer-Specific Monitoring of SialylatedFrontiers in molecular biosciences · 2021Article
- Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation.Molecular & cellular proteomics : MCP · 2021Review
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- A Linkage-specific Sialic Acid Labeling Strategy Reveals Different Site-specific Glycosylation Patterns in SARS-CoV-2 Spike Protein Produced in CHO and HEK Cell Substrates.Frontiers in chemistry · 2021Article
- Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure-function relationships.Mass spectrometry reviews · 2020Review
- Identifying Sialylation Linkages at the Glycopeptide Level by Glycosyltransferase Labeling Assisted Mass Spectrometry (GLAMS).Analytical chemistry · 2020Article
- Glycomics studies using sialic acid derivatization and mass spectrometry.Nature reviews. Chemistry · 2020Review
- Quantification of the α2-6 Sialic Acid Linkage in Branched N-Glycan Structures with Capillary Nanogel Electrophoresis.Analytical chemistry · 2020Article
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Authors and funding
5 authors.
Funding
Abstract
Mass spectrometric analysis of intact glycopeptides can reveal detailed information about glycosite, glycan structural features, and their heterogeneity. Sialyl glycopeptides can be positively, negatively, or neutrally charged depending on pH of their buffer solution and ionization conditions. To detect sialoglycopeptides, a negative-ion mode mass spectrometry may be applied with a minimal loss of sialic acids, although the positively charged or neutral glycopeptides may be excluded. Alternatively, the sialyl glycopeptides can be identified using positive-ion mode analysis by doping a high concentration of sodium salts to the analytes. Although manipulation of unmodified sialoglycopeptides can be useful for analysis of samples, less than optimal ionization, facile loss of sialyl and unfavorable ionization of accompanying non-sialyl peptides make such strategies suboptimal. Currently available chemical derivatization methods, while stabilizing for sialic acid, mask sialic acid linkage configuration. Here, we report the development of a novel approach to neutralize sialic acids via sequentially chemical modification that also reveals their linkage configuration, often an important determinant in biological function. This method utilizes several components to facilitate glycopeptide identification. These include the following: solid phase derivatization, enhanced ionization of sialoglycopeptides, differentiation of sialic acid linkage, and enrichment of the modified glycopeptides by hydrophilic interaction liquid chromatography. This technology can be used as a tool for quantitative analysis of protein sialylation in diseases with determination of sialic acid linkage configuration. Graphical Abstract ᅟ.
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