Sialo-glycoproteome of Human lung cancer cell by LC-MSMS

Alterations in protein glycosylation, especially the terminal sialylation, are closely correlated with physiological and pathological regulation. Due to the low ionization efficiency of sialo-glycopeptides and frequently observed dissociation of sialic acid residues during mass spectrometry analysis, tools to enrich the sialo-glycopeptides are essential to enhance detection sensitivity and identification efficiency in sialo-glycoproteomics. In this study, we present the first application of zwitterionic hydrophilic interaction chromatography (ZIC-cHILIC) material in StageTip for simultaneous enrichment and fractionation of intact glycopeptides at proteome scale. With the demonstrated enrichment specificity and identification depth, the stepwise-ZIC-cHILIC can be an efficient enrichment method for the discovery of glycosylation sites and native glycotope for many sample types.