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Updated: Feb 5, 2026
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Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
Published on: April 21, 2017
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Advances in mass spectrometry-based glycoproteomics
Aiying Yu1, Jingfu Zhao1, Wenjing Peng1
1Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, USA.
Electrophoresis
|September 12, 2018
Summary
Protein glycosylation, a vital post-translational modification (PTM), is crucial for biological processes but challenging to study. This review highlights recent advances in glycoproteomics for accurate characterization of protein glycosylation.
Area of Science:
- Biochemistry
- Molecular Biology
- Analytical Chemistry
Background:
- Protein glycosylation is a critical post-translational modification (PTM) involved in numerous biological functions.
- Aberrant glycosylation patterns are linked to various human diseases.
- Studying protein glycosylation is challenging due to low abundance, site heterogeneity, and poor glycopeptide ionization.
Purpose of the Study:
- To review recent advancements in glycoproteomics techniques for characterizing protein glycosylation.
- To provide an overview of methods developed between 2012 and 2018.
Main Methods:
- Glycopeptide enrichment strategies.
- Metabolic labeling techniques.
- Glycopeptide derivatization methods.
- Mass spectrometry (MS) techniques.
- Bioinformatics tools for data analysis.
Main Results:
- Development of sensitive and accurate MS-based approaches for glycoproteomics.
- Improved methods for enrichment, labeling, and derivatization of glycopeptides.
- Enhanced capabilities for quantitative and qualitative characterization of glycoproteins.
Conclusions:
- Recent developments have significantly improved the ability to study protein glycosylation.
- Glycoproteomics is essential for understanding the role of glycosylation in health and disease.
- Continued innovation in MS and bioinformatics will further advance the field.
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