Effective Assignment of α2,3/α2,6‐Sialic Acid Isomers by LC‐MS/MS‐Based Glycoproteomics |
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Authors: | Dr Christian Pett Dr Waqas Nasir Dr Carina Sihlbom M?Sc Britt‐Marie Olsson M?Sc Vanessa Caixeta Dr Manuel Schorlemer Dr René P Zahedi Prof Göran Larson Dr Jonas Nilsson Prof Ulrika Westerlind |
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Institution: | 1. Leibniz-Institut für Analytische Wissenschaften–ISAS–e.V., Dortmund, Germany;2. Department of Chemistry, Ume? University, Ume?, Sweden;3. Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden;4. Thermo Fischer Scientific, Bremen, Germany;5. Proteomics Core Facility, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden;6. Segal Cancer Proteomics Centre, Lady Davis Institute, Jewish General Hospital, McGill University, Montreal, Quebec, Canada |
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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. |
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Keywords: | glycopeptides glycosylation isomers mass spectrometry sialic acids |
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