Intact glycopeptide characterization using mass spectrometry

被引:51
作者
Cao, Li [1 ]
Qu, Yi [2 ]
Zhang, Zhaorui [3 ]
Wang, Zhe [4 ]
Prytkova, Iya [4 ]
Wu, Si [4 ]
机构
[1] GSK, Pharma Res & Dev, R&D Platform Technol & Sci, King Of Prussia, PA USA
[2] Evans Analyt Grp, ChemEco Div, Hercules, CA USA
[3] AbbVie, Proc Res & Dev, N Chicago, IL USA
[4] Univ Oklahoma, Dept Chem & Biochem, 101 Stephenson Pkwy,Room 2210, Norman, OK 73019 USA
关键词
Glycosylation; glycopeptide; post-translational modification; LC-MS; MS; proteomics; bioinformatics; SITE-SPECIFIC GLYCOSYLATION; PROSTATE-SPECIFIC ANTIGEN; PROTEIN GLYCOSYLATION; O-GLYCOSYLATION; MONOCLONAL-ANTIBODIES; LIQUID-CHROMATOGRAPHY; LINKED GLYCOPEPTIDES; HYDRAZIDE CHEMISTRY; N-GLYCOPROTEOME; LC-MS/MS;
D O I
10.1586/14789450.2016.1172965
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Glycosylation is one of the most prominent and extensively studied protein post-translational modifications. However, traditional proteomic studies at the peptide level (bottom-up) rarely characterize intact glycopeptides (glycosylated peptides without removing glycans), so no glycoprotein heterogeneity information is retained. Intact glycopeptide characterization, on the other hand, provides opportunities to simultaneously elucidate the glycan structure and the glycosylation site needed to reveal the actual biological function of protein glycosylation. Recently, significant improvements have been made in the characterization of intact glycopeptides, ranging from enrichment and separation, mass spectroscopy (MS) detection, to bioinformatics analysis. In this review, we recapitulated currently available intact glycopeptide characterization methods with respect to their advantages and limitations as well as their potential applications.
引用
收藏
页码:513 / 522
页数:10
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