Glycosylation is one of the most common and important types of protein post-translational modifications in mammalian cells. To decode the protein glycosylation, it is highly important to enrich glycopeptides or separate glycans from complex biosamples. Hydrophilic interaction liquid interaction chromatography (HILIC) has inherent advantages in the separation of hydrophilic substances and glycopeptide enrichment. Conventional HILIC display unbiased binding with the hydrophilic solutes, leading to unsatisfactory enrichment selectivity for glycopeptides. In recent three years, many novel HILIC materials, including histidine, dipeptide, maltose, and amide-based ones, were developed and displayed either specific binding capacities toward sialylated glycopeptides, or substantially stronger retention toward neutral glycopeptides. Therefore, HILIC has grown up to be a high-efficiency method for collecting both glycosylation sites and glycan structural information simultaneously. In the review, recent breakthrough of HILIC materials applied to glycopeptide enrichment and glycan separation is summarized, and the future development tendency of the HILIC is suggested. 

Recent advances in hydrophilic interaction liquid interaction chromatography materials for glycopeptide enrichment and glycan separation

Guangyan Qing, Jingyu Yan, Xiangnan He, Xiuling Li**, Xinmiao Liang*

Trends in Analytical Chemistry, 2020, 124, 115570.

DOI: 10.1016/j.trac.2019.06.020