| Literature DB >> 29742324 |
Christian Pett1,2, Waqas Nasir3,4, Carina Sihlbom5, Britt-Marie Olsson5, Vanessa Caixeta1, Manuel Schorlemer1,2, René P Zahedi1,6, Göran Larson3, Jonas Nilsson3, Ulrika Westerlind1,2.
Abstract
Distinct structural changes of the α2,3/α2,6-sialic acid glycosidic linkages on glycoproteins are of importance in cancer biology, inflammatory diseases, and virus tropism. Current glycoproteomic methodologies are, however, not amenable toward high-throughput characterization of sialic acid isomers. To enable such assignments, a mass spectrometry method utilizing synthetic model glycopeptides for the analysis of oxonium ion intensity ratios was developed. This method was successfully applied in large-scale glycoproteomics, thus allowing the site-specific structural characterization of sialic acid isomers.Entities:
Keywords: glycopeptides; glycosylation; isomers; mass spectrometry; sialic acids
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Year: 2018 PMID: 29742324 DOI: 10.1002/anie.201803540
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336