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Journal Article

Distinguishing N-acetylneuraminic acid linkage isomers on glycopeptides by ion mobility-mass spectrometry

MPS-Authors
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Hinneburg,  Hannes
Daniel Kolarich, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Hofmann,  Johanna
Department of Biology, Chemistry, Pharmacy, Freie Universität Berlin;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Varón Silva,  Daniel
Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Seeberger,  Peter H.
Department of Biology, Chemistry, Pharmacy, Freie Universität Berlin;
Peter H. Seeberger, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Pagel,  Kevin
Department of Biology, Chemistry, Pharmacy, Freie Universität Berlin;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Kolarich,  Daniel
Daniel Kolarich, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Hinneburg, H., Hofmann, J., Struwe, W. B., Thader, A., Altmann, F., Varón Silva, D., et al. (2016). Distinguishing N-acetylneuraminic acid linkage isomers on glycopeptides by ion mobility-mass spectrometry. Chemical Communications, 52(23), 4381-4384. doi:10.1039/C6CC01114D.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-1E81-8
Abstract
Differentiating the structure of isobaric glycopeptides represents a major challenge for mass spectrometry-based characterisation techniques. Here we show that the regiochemistry of the most common N-acetylneuraminic acid linkages of N-glycans can be identified in a site-specific manner from individual glycopeptides using ion mobility-mass spectrometry analysis of diagnostic fragment ions.