Literature DB >> 26780731

Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides.

Jonas Nilsson1.   

Abstract

The use of liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS(n)) for the glycoproteomic characterization of glycopeptides is a growing field of research. The N- and O-glycosylated peptides (N- and O-glycopeptides) analyzed typically originate from protease-digested glycoproteins where many of them are expected to be biomedically important. Examples of LC-MS(2) and MS(3) fragmentation strategies used to pursue glycan structure, peptide identity and attachment-site identification analyses of glycopeptides are described in this review. MS(2) spectra, using the CID and HCD fragmentation techniques of a complex biantennary N-glycopeptide and a core 1 O-glycopeptide, representing two examples of commonly studied glycopeptide types, are presented. A few practical tips for accomplishing glycopeptide analysis using reversed-phase LC-MS(n) shotgun proteomics settings, together with references to the latest glycoproteomic studies, are presented.

Entities:  

Keywords:  Collision-induced dissociation; Electron capture dissociation; Electron transfer dissociation; Glycopeptides; Glycoproteomics; Higher-energy collisional dissociation; Mass spectrometry; Oxonium ions

Mesh：

Substances：

Year:  2016        PMID： 26780731     DOI： 10.1007/s10719-016-9649-3

Source DB:  PubMed          Journal:  Glycoconj J        ISSN： 0282-0080            Impact factor:   2.916


  100 in total

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Review 3.  Automated glycopeptide analysis--review of current state and future directions.

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4.  Higher energy collision dissociation (HCD) product ion-triggered electron transfer dissociation (ETD) mass spectrometry for the analysis of N-linked glycoproteins.

Authors:  Charandeep Singh; Cleidiane G Zampronio; Andrew J Creese; Helen J Cooper
Journal:  J Proteome Res       Date:  2012-08-06       Impact factor: 4.466

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Authors:  Morten Thaysen-Andersen; Nicolle H Packer
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6.  O-Mannose and O-N-acetyl galactosamine glycosylation of mammalian α-dystroglycan is conserved in a region-specific manner.

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7.  O-linked glycosylation of the mucin domain of the herpes simplex virus type 1-specific glycoprotein gC-1 is temporally regulated in a seed-and-spread manner.

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9.  Distinctive MS/MS Fragmentation Pathways of Glycopeptide-Generated Oxonium Ions Provide Evidence of the Glycan Structure.

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10.  Site-specific N-glycosylation analysis of human immunoglobulin e.

Authors:  Rosina Plomp; Paul J Hensbergen; Yoann Rombouts; Gerhild Zauner; Irina Dragan; Carolien A M Koeleman; André M Deelder; Manfred Wuhrer
Journal:  J Proteome Res       Date:  2013-12-13       Impact factor: 4.466
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  18 in total

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2.  Sensitive and fast characterization of site-specific protein glycosylation with capillary electrophoresis coupled to mass spectrometry.

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Review 3.  Maturing Glycoproteomics Technologies Provide Unique Structural Insights into the N-glycoproteome and Its Regulation in Health and Disease.

Authors:  Morten Thaysen-Andersen; Nicolle H Packer; Benjamin L Schulz
Journal:  Mol Cell Proteomics       Date:  2016-02-29       Impact factor: 5.911

4.  Glycoproteomics Technologies in Glycobiotechnology.

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5.  Precursor ion survival energies of protonated N-glycopeptides and their weak dependencies on high mannose N-glycan composition in collision-induced dissociation.

Authors:  Forouzan Aboufazeli; Eric D Dodds
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6.  Parallel Determination of Polypeptide and Oligosaccharide Connectivities by Energy-Resolved Collison-Induced Dissociation of Protonated O-Glycopeptides Derived from Nonspecific Proteolysis.

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Review 7.  Mass Spectrometry Approaches to Glycomic and Glycoproteomic Analyses.

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Review 8.  Recent advances in mass spectrometric analysis of glycoproteins.

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9.  Distinctive and Complementary MS2 Fragmentation Characteristics for Identification of Sulfated Sialylated N-Glycopeptides by nanoLC-MS/MS Workflow.

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Journal:  J Am Soc Mass Spectrom       Date:  2018-04-11       Impact factor: 3.109

Review 10.  Chemical Glycoproteomics.

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