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题名: Hydrophilic Interaction Chromatography Based Enrichment of Glycopeptides by Using Click Maltose: A Matrix with High Selectivity and Glycosylation Heterogeneity Coverage
作者: Yu, Long1;  Li, Xiuling1;  Guo, Zhimou1;  Zhang, Xiuli1;  Liang, Xinmiao1
通讯作者: 梁鑫淼
关键词: analytical methods ;  glycopeptides ;  glycoproteins ;  mass spectrometry
刊名: CHEMISTRY-A EUROPEAN JOURNAL
发表日期: 2009
DOI: 10.1002/chem.200902370
卷: 15, 期:46, 页:12618-12626
收录类别: SCI
文章类型: Article
部门归属: 18
项目归属: 1803
产权排名: 1;1
WOS标题词: Science & Technology ;  Physical Sciences
类目[WOS]: Chemistry, Multidisciplinary
研究领域[WOS]: Chemistry
英文摘要: Glycosylation analysis based on mass spectrometry (MS) of glycopeptides requires the isolation of glycopeptides from complex glycoprotein digests to facilitate structural determination of the glycopeptides. To this end, hydrophilic interaction chromatography (HILIC)-based methods have been developed to selectively enrich glycopeptides by utilizing the hydrophilicity of the glycans. However, the application of these methods is limited by the medium selectivity of HILIC matrices. To improve the effectiveness of HILIC-based methods, we introduced a customized hydrophilic matrix named "click maltose" and characterized its selectivity and glycosylation heterogeneity coverage. In the selectivity assessment, the non-glycopeptides causing ion suppression to the glycopeptides were effectively removed by click maltose, leading to the identification of 27 glycopeptides in the fractions enriched from human serum immunoglobulin G digest, compared to 13 glycopeptides enriched using Sepharose CL-6B, a commercially available matrix. For the assessment of glycosylation heterogeneity coverage, more than 140 glycopeptides covering all the five glycosites of human serum alpha(1)-acid glycoprotein were captured using click maltose. Click maltose was synthesized by linking alkynyl-derivatized maltose to azide-derivatized silica through click chemistry. The resulting flexible saccharide chain structure remarkably enhances the hydrogen-bonding interactions between the glycans of the glycopeptides and the matrix, which are responsible for the increased selectivity and glycosylation heterogeneity coverage of click maltose.
关键词[WOS]: LECTIN AFFINITY-CHROMATOGRAPHY ;  INTERACTION LIQUID-CHROMATOGRAPHY ;  TANDEM MASS-SPECTROMETRY ;  PROTEIN GLYCOSYLATION ;  IMMUNOGLOBULIN-G ;  UNDERIVATIZED OLIGOSACCHARIDES ;  GLYCOPROTEIN GLYCOSYLATION ;  ALPHA-1-ACID GLYCOPROTEIN ;  ZWITTERIONIC TYPE ;  N-GLYCOPEPTIDES
语种: 英语
原文出处: 查看原文
WOS记录号: WOS:000272509500013
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/102677
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China

Recommended Citation:
Yu, Long,Li, Xiuling,Guo, Zhimou,et al. Hydrophilic Interaction Chromatography Based Enrichment of Glycopeptides by Using Click Maltose: A Matrix with High Selectivity and Glycosylation Heterogeneity Coverage[J]. CHEMISTRY-A EUROPEAN JOURNAL,2009,15(46):12618-12626.
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