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Effective Assignment of alpha 2,3/alpha 2,6-Sialic Acid Isomers by LC-MS/MS-Based Glycoproteomics

Journal article
Authors C. Pett
W. Nasir
Carina Sihlbom
Britt-Marie Olsson
V. Caixeta
M. Schorlemer
R. P. Zahedi
G. Larson
J. Nilsson
U. Westerlind
Published in Angewandte Chemie International Edition
Volume 57
Issue 30
Pages 9320-9324
ISSN 1433-7851
Publication year 2018
Published at Core Facilities, Proteomics
Pages 9320-9324
Language en
Links dx.doi.org/10.1002/anie.201803540
Keywords glycopeptides, glycosylation, isomers, mass spectrometry, sialic acids, mass-spectrometry, damsela alpha-2,6-sialyltransferase, glycan, structure, linkage isomers, n-glycans, glycopeptides, identification, derivatization, strategy, sialyltransferase, Chemistry
Subject categories Biochemistry and Molecular Biology

Abstract

Distinct structural changes of the alpha 2,3/alpha 2,6-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.

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