Analytical platforms and method development
Our group develops advanced glycomics technology. For mass spectrometry glycomics analyses we try and push the boundaries regarding sensitivity and throughput. We aim at grasping the complexity of the human glycome including protein glycosylation (N- and O-glycans) as well as glycosphingolipids. We develop approaches for the full structural definition of glycans by combining mass spectrometry with various separation and derivatization techniques.


Our group has a profound interest in Glycoimmunology, with a particular focus on antibody glycosylation. Human immunoglobulin G is the best studied group of glycoproteins with respect to its protein structure, but also regarding its posttranslational modifications, including glycosylation. We are intrigued by the vast influence of IgG glycosylation changes on the function of these biomolecules, and study the role and biomarker potential of antibody glycosylation in various disease settings.


Many developmental steps are known to involve glycosylation changes. At an systemic level, we aim at mapping the changes of the glycome in altered physiological states including developmental steps in early childhood, adolescence, and (healthy) aging. At a cellular level, we dissect the role of glycans as modulators and effectors of cellular differentiation.


Glycosylation in cancer is another key research are of our group. We analyze specific glycans of cancer cells and tumor tissues, characterize glycosylated, circulating tumor antigens. We study the contribution of glycans to tumor progression and metastasis. We evaluate emerging tumor-associated carbohydrate antigens (TACAs) for diagnostic purposes as well as therapeutic targets.

Characterization of biopharmaceuticals

Glycosylation is a key determinant of the efficacy and safety of biopharmaceuticals. Together with other modifications, glycosylation defines the proteoform makeup of biopharmaceutical products. In collaboration with biopharma, we develop and apply mass spectrometry-based methods for proteoform-resolved pharmacokinetic analyses and for proteoform-resolved interaction analyses to gain molecular insights into the contribution glycosylation and other modifications to the fate, efficacy and safety of these highly complex drugs.

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