Hydrophilic Interaction Liquid Chromatography (HILIC) Enrichment of Glycopeptides Using PolyHYDROXYETHYL A

Mona Goli; Peilin Jiang; Mojibola Fowowe; Md Abdul Hakim; Yehia Mechref

doi:10.1007/978-1-0716-3666-4_16

Hydrophilic Interaction Liquid Chromatography (HILIC) Enrichment of Glycopeptides Using PolyHYDROXYETHYL A

Methods Mol Biol. 2024:2762:267-280. doi: 10.1007/978-1-0716-3666-4_16.

Authors

Mona Goli¹, Peilin Jiang¹, Mojibola Fowowe¹, Md Abdul Hakim¹, Yehia Mechref²

Affiliations

¹ Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, USA.
² Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, USA. Yehia.Mechref@ttu.edu.

PMID: 38315371
DOI: 10.1007/978-1-0716-3666-4_16

Abstract

Glycosylation of proteins is an important post-translational modification that plays a role in a wide range of biological processes, including immune response, intercellular signaling, inflammation, and host-pathogen interaction. Abnormal protein glycosylation has been correlated with various diseases. However, the study of protein glycosylation remains challenging due to its low abundance, microheterogeneity of glycosylation sites, and low ionization efficiency. During the past decade, several methods for enrichment and for isolation of glycopeptides from biological samples have been developed and successfully employed in glycoproteomics research. In this chapter, we discuss the sample preparation protocol and the strategies for effectively isolating and enriching glycopeptides from biological samples, using PolyHYDROXYETHYL A as a hydrophilic interaction liquid chromatography (HILIC) enrichment technique.

Keywords: Glycopeptides; HILIC enrichment; LC-MS/MS; TopTip C18 desalting.

MeSH terms

Chromatography, Liquid / methods
Glycopeptides* / analysis
Glycosylation
Hydrophobic and Hydrophilic Interactions
Protein Processing, Post-Translational*

Substances

Glycopeptides