DICP OpenIR
Hydrophilic Interaction Chromatography Based Enrichment of Glycopeptides by Using Click Maltose: A Matrix with High Selectivity and Glycosylation Heterogeneity Coverage
Yu, Long; Li, Xiuling; Guo, Zhimou; Zhang, Xiuli; Liang, Xinmiao; Liang XM(梁鑫淼)
KeywordAnalytical Methods Glycopeptides Glycoproteins Mass Spectrometry
Source PublicationCHEMISTRY-A EUROPEAN JOURNAL
2009
DOI10.1002/chem.200902370
Volume15Issue:46Pages:12618-12626
Indexed BySCI
SubtypeArticle
Department18
Funding Project1803
Contribution Rank1;1
WOS HeadingsScience & Technology ; Physical Sciences
WOS SubjectChemistry, Multidisciplinary
WOS Research AreaChemistry
WOS KeywordLECTIN AFFINITY-CHROMATOGRAPHY ; INTERACTION LIQUID-CHROMATOGRAPHY ; TANDEM MASS-SPECTROMETRY ; PROTEIN GLYCOSYLATION ; IMMUNOGLOBULIN-G ; UNDERIVATIZED OLIGOSACCHARIDES ; GLYCOPROTEIN GLYCOSYLATION ; ALPHA-1-ACID GLYCOPROTEIN ; ZWITTERIONIC TYPE ; N-GLYCOPEPTIDES
AbstractGlycosylation 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.
Language英语
URL查看原文
WOS IDWOS:000272509500013
Citation statistics
Cited Times:122[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/102677
Collection中国科学院大连化学物理研究所
Corresponding AuthorLiang XM(梁鑫淼)
AffiliationChinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
Recommended Citation
GB/T 7714
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.
APA Yu, Long,Li, Xiuling,Guo, Zhimou,Zhang, Xiuli,Liang, Xinmiao,&梁鑫淼.(2009).Hydrophilic Interaction Chromatography Based Enrichment of Glycopeptides by Using Click Maltose: A Matrix with High Selectivity and Glycosylation Heterogeneity Coverage.CHEMISTRY-A EUROPEAN JOURNAL,15(46),12618-12626.
MLA Yu, Long,et al."Hydrophilic Interaction Chromatography Based Enrichment of Glycopeptides by Using Click Maltose: A Matrix with High Selectivity and Glycosylation Heterogeneity Coverage".CHEMISTRY-A EUROPEAN JOURNAL 15.46(2009):12618-12626.
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