文摘
Protein glycosylation plays critical roles in the regulation of diverse biological processes, and determination of glycan structure鈥揻unction relationships is important to better understand these events. However, characterization of glycan and glycopeptide structural isomers remains challenging and often relies on biosynthetic pathways being conserved. In glycoproteomic analysis with liquid chromatography鈥搕andem mass spectrometry (LC鈥揗S/MS) using collision-induced dissociation (CID), saccharide oxonium ions containing N-acetylhexosamine (HexNAc) residues are prominent. Through analysis of beam-type CID spectra and ion trap CID spectra of synthetic and natively derived N- and O-glycopeptides, we found that the fragmentation patterns of oxonium ions characteristically differ between glycopeptides terminally substituted with GalNAc伪1-O-, GlcNAc尾1-O-, Gal尾3GalNAc伪1-O-, Gal尾4GlcNAc尾-O-, and Gal尾3GlcNAc尾-O- structures. The difference in the oxonium ion fragmentation profiles of such glycopeptides may thus be used to distinguish among these glycan structures and could be of importance in LC鈥揗S/MS-based glycoproteomic studies.r>Keywords:
glycoproteomics; oxonium ion; LC鈭扢S/MS; glycopeptide; O-glycosylation