This review covers recent developments in glycosaminoglycan (GAG) analysis via mass spectrometry (MS). GAGs participate in a variety of biological functions, including cellular communication, wound healing, and anticoagulation, and are important targets for structural characterization. GAGs exhibit a diverse range of structural features due to the variety of O- and N-sulfation modifications and uronic acid C-5 epimerization that can occur, making their analysis a challenging target. Mass spectrometry approaches to the structure assignment of GAGs have been widely investigated, and new methodologies remain the subject of development. Advances in sample preparation, tandem MS techniques (MS/MS), online separations, and automated analysis software have advanced the field of GAG analysis. These recent developments have led to remarkable improvements in the precision and time efficiency for the structural characterization of GAGs.
CITATION STYLE
Pepi, L. E., Sanderson, P., Stickney, M., & Amster, I. J. (2021). Developments in mass spectrometry for glycosaminoglycan analysis: A review. Molecular and Cellular Proteomics. American Society for Biochemistry and Molecular Biology Inc. https://doi.org/10.1074/MCP.R120.002267
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