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Effective Assignment of α2,3/α2,6‐Sialic Acid Isomers by LC‐MS/MS‐Based Glycoproteomics
Author(s) -
Pett Christian,
Nasir Waqas,
Sihlbom Carina,
Olsson BrittMarie,
Caixeta Vanessa,
Schorlemer Manuel,
Zahedi René P.,
Larson Göran,
Nilsson Jonas,
Westerlind Ulrika
Publication year - 2018
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201803540
Subject(s) - glycoproteomics , oxonium ion , sialic acid , chemistry , glycosidic bond , glycan , mass spectrometry , biochemistry , glycoprotein , characterization (materials science) , glycosylation , computational biology , chromatography , ion , organic chemistry , biology , nanotechnology , enzyme , materials science
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.