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N-linked protein glycosylation is the most common post-translational modification(PTM).However,characterizing this PTM is difficult for mass spectrometry(MS)because of low concentration of glycopeptides and suppression effect of non-glycosylated peptides.Therefore it is imperative to enrich glycopeptides prior to MS analysis.Hydrophilic interaction chromatography(HILIC)in solid phase extraction(SPE)mode has been increasingly employed to enrich glycopeptides in the last few years.However,the enrichment selectivity for glycopeptides is moderate because of co-elution of non-glycosylated peptides containing multiple serine/threonine residues or larger molecular weight.In order to improve the enrichment selectivity of glycopeptides,several novel HILIC-based materials were synthesized in our group and applied to enrich N-linked glycopeptides.Compared to commercial HILIC materials,the synthesized materials exhibited remarkably higher selectivity for glycopeptides.We believe these HILIC materials will become promising tools in glycoproteomic studies.