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Göteborgs universitets publikationer

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

Författare och institution:
Jonas Nilsson (Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin)
Publicerad i:
Glycoconjugate Journal, 33 ( 3 ) s. 261-272
ISSN:
0282-0080
Publikationstyp:
Artikel, refereegranskad vetenskaplig
Publiceringsår:
2016
Språk:
engelska
Fulltextlänk:
Sammanfattning (abstract):
The use of liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MSn) 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-MS2 and MS3 fragmentation strategies used to pursue glycan structure, peptide identity and attachment-site identification analyses of glycopeptides are described in this review. MS2 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-MSn shotgun proteomics settings, together with references to the latest glycoproteomic studies, are presented.
Ämne (baseras på Högskoleverkets indelning av forskningsämnen):
MEDICIN OCH HÄLSOVETENSKAP ->
Klinisk medicin
Nyckelord:
Glycoproteomics, Glycopeptides, Oxonium ions, Mass spectrometry, Collision-induced dissociation, Higher-energy collisional dissociation, Electron capture dissociation, Electron transfer dissociation, electron-transfer dissociation, human cerebrospinal-fluid, n-glycosylation analysis, c-trap dissociation, collision-induced, dissociation, site-specific characterization, o-glycosylation, lc-ms/ms, protein glycosylation, glycan structure
Postens nummer:
238861
Posten skapad:
2016-07-04 12:03

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