【摘 要】
：
Characterization of protein glycosylation requires highly specific methods for the enrichment of glycopeptides because of their sub-stoichiometric glycosylation-site occupancy.The hydrophilic affinity
【机 构】
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Key Lab of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chines
【出 处】
：
第2届大连国际色谱学术报告会、第37届国际高效液相色谱及相关技术会议、第18届全国色谱学术报告会
论文部分内容阅读
Characterization of protein glycosylation requires highly specific methods for the enrichment of glycopeptides because of their sub-stoichiometric glycosylation-site occupancy.The hydrophilic affinity based strategy has attracted more attention, owing to its broad glycan specificity, good reproducibility, and compatibility with mass spectrometric (MS) analysis.Several polar matrices have emerged for hydrophilic interaction chromatography (HILIC) approaches, including sepharose, cellulose, ZIC-HILIC and titania.Here, we present the solid-phase extraction (SPE) utility of zirconia coated mesoporous silica (ZrO2/MPS) microspheres for glycopeptide isolation prior to MS analysis.The high specificity of this SPE approach was demonstrated by the enrichment of glycopeptides from the digests of model glycoproteins in HILIC mode.ZrO2/MPS microspheres show superior selectivity and glycosylation heterogeneity coverage for glycopeptide enrichment to conventional sepharose.Furthermore, digested mixtures of the phosphoprotein α-casein and IgG were also treated with ZrO2/MPS HILIC SPE materials, which exhibited glycopeptides could be effectively enriched with interference from phosphorylated peptides.
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