ArticleJournal of biomolecular techniques : JBT2016
Resolving Isomeric Glycopeptide Glycoforms with Hydrophilic Interaction Chromatography (HILIC).
Article in Journal of biomolecular techniques : JBT, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Absolute Quantitation of Phosphopeptides and Glycopeptides Using Coulometric Mass Spectrometry.ACS measurement science au · 2025Article
- Optimization of glycopeptide enrichment techniques for the identification of clinical biomarkers.Expert review of proteomics · 2024Review
- LC-MS/MS of isomeric N-and O-glycopeptides on mesoporous graphitized carbon column.Analytica chimica acta · 2024Article
- Standards-Free Absolute Quantitation of Oxidizable Glycopeptides by Coulometric Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Decoding the glycoproteome: a new frontier for biomarker discovery in cancer.Journal of hematology & oncology · 2024Review
- O-Glycoproteomics Sample Preparation and Analysis Using NanoHPLC and Tandem MS.Methods in molecular biology (Clifton, N.J.) · 2024Article
- LC-MS/MS Quantitation of HILIC-EnrichedBiomolecules · 2023Article
- Glycoproteomics-Compatible MS/MS-Based Quantification of Glycopeptide Isomers.Analytical chemistry · 2023Article
- Methods for quantification of glycopeptides by liquid separation and mass spectrometry.Mass spectrometry reviews · 2023Review
- Quantitative clinical glycomics strategies: A guide for selecting the best analysis approach.Mass spectrometry reviews · 2022Review
- Optimized Sample Preparation and Microscale Separation Methods for High-Sensitivity Analysis of Hydrophilic Peptides.Molecules (Basel, Switzerland) · 2022Article
- Prediction of Intact N-Glycopeptide Retention Time Windows in Hydrophilic Interaction Liquid Chromatography.Molecules (Basel, Switzerland) · 2022Article
- Mass Spectrometry-Based Techniques to Elucidate the Sugar Code.Chemical reviews · 2022Review
- StrucGP: de novo structural sequencing of site-specific N-glycan on glycoproteins using a modularization strategy.Nature methods · 2021Article
- Comparison of human IgG glycopeptides separation using mixed-mode hydrophilic interaction/ion-exchange liquid chromatography and reversed-phase mode.Analytical and bioanalytical chemistry · 2021Article
- Article
- Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021Review
- Glycine additive facilitates site-specific glycosylation profiling of biopharmaceuticals by ion-pairing hydrophilic interaction chromatography mass spectrometry.Analytical and bioanalytical chemistry · 2021Article
- State-of-the-Art Glycomics Technologies in Glycobiotechnology.Advances in biochemical engineering/biotechnology · 2021Article
- Glucose unit index (GUI) of permethylated glycans for effective identification of glycans and glycan isomers.The Analyst · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The ability to resolve glycans while attached to tryptic peptides would greatly facilitate glycoproteomics, as this would enable site-specific glycan characterization. Peptide/glycopeptide separations are typically performed using reversed-phase liquid chromatography (RPLC), where retention is driven by hydrophobic interaction. As the hydrophilic glycans do not interact significantly with the RPLC stationary phase, it is difficult to resolve glycopeptides that differ only in their glycan structure, even when these differences are large. Alternatively, glycans interact extensively with the stationary phases used in hydrophilic interaction chromatography (HILIC), and consequently, differences in glycan structure have profound chromatographic shifts in this chromatographic mode. Here, we evaluate HILIC for the separation of isomeric glycopeptide mixtures that have the same peptide backbone but isomeric glycans. Hydrophilic functional groups on both the peptide and the glycan interact with the HILIC stationary phase, and thus, changes to either of these moieties can alter the chromatographic behavior of a glycopeptide. The interactive processes permit glycopeptides to be resolved from each other based on differences in their amino acid sequences and/or their attached glycans. The separations of glycans in HILIC are sufficient to permit resolution of isomeric N-glycan structures, such as sialylated N-glycan isomers differing in α2-3 and α2-6 linkages, while these glycans remain attached to peptides.
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