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preprint hCG glycosylation chemrXiv 03 0302021.pdf (1.16 MB)

Exploring the Chemical Space of Protein Glycosylation in Noncovalent Protein Complexes: An Expedition Along Different Structural Levels of Human Chorionic Gonadotropin Employing Mass Spectrometry

submitted on 04.03.2021, 08:13 and posted on 05.03.2021, 04:33 by Maximilian Lebede, Fiammetta di Marco, Wolfgang Esser-Skala, René Hennig, Therese Wohlschlager, Christian G. Huber
Exploration of a highly glycosylated non-covalent protein comples by mass spectreometry is a challenging task due to isobarisicy of the majority of glycoforms. Integration of data from multiple structural levels (released glycan-glycopeptide-protein subunit-protein complex) by means of computational algorithms permits unraveling the hidden diversity of the human chorionic gonadotropin heterodimer, constituting the base for the study of complex glycosylated protein assemblies.


This work was funded by the Austrian Federal Ministry for Digital and Economic Affairs, the National Foundation of Research, Technology, and Development, a Start-up Grant of the State of Salzburg, as well as the Austrian Science Fund (W1213).


Email Address of Submitting Author


University of Salzburg



ORCID For Submitting Author


Declaration of Conflict of Interest

Novartis AG / Sandoz GmbH as well as Thermo Fisher Scientific provide financial support for the Christian Doppler Laboratory for Innovative Tools for Biosimilar Characterization. René Hennig is employee of glyXera GmbH, Magdeburg, Germany. The salaries of Wolfgang Esser-Skala and Therese Wohlschlager are fully funded; Christian G. Huber’s salary is partly funded by the Christian Doppler Laboratory for Biosimilar Characterization. The authors declare no other competing financial interest.