We are pleased to announce that a successful collaboration with the Department of Biosciences at the University of Salzburg and the Christian Doppler Laboratory for Innovative Tools for Biosimilar Characterization at the University of Salzburg has resulted in publishing an article in Analytical Chemistry with the title “Exploring the Chemical Space of Protein Glycosylation in Noncovalent Protein Complexes: An Expedition along Different Structural Levels of Human Chorionic Gonadotropin by Employing Mass Spectrometry“.

The detailed characterization and control of protein glycosylation has become of utmost importance in the biopharmaceutical industry since this posttranslational modification of proteins is universally recognized as a critical quality attribute. Due to its influence on the structure and function of proteins, it is essential to carefully monitor protein glycosylation during the development process of new biopharmaceutical drugs and in later stages of a product’s life cycle. Therefore, various very powerful analytical techniques were developed, ranging from broad, fast, and simple characterization, up to slow, but detailed elucidation of minute details. Combining several analytical methods, utilizing their individual benefits, turned out to be the most successful strategy for a detailed characterization.

Inside the published article we present a detailed characterization of one of the most complex biopharmaceuticals on the market, the recombinant human chorionic gonadotropin (hCG). Especially for mass spectrometry (MS) based analysis of complex intact glycoproteins (or glycopeptides thereof), the vast diversity of possible protein-glycan combinations (driven by the complexity of glycans) turned out to dramatically increase the computing time necessary for the interpretation of mass spectra. To reduce computing time, an initial global characterization of the hCG N-glycome was performed by xCGE-LIF. The resulting glycan list was used to search against a targeted set of defined N-glycan structures as variable protein/peptide modifications, which greatly reduced the search space, and thereby the computing time. The combination of these two powerful methods, xCGE-LIF and MS, made it possible to explore the chemical space of the rather complex hCG glycosylation in a relatively short amount of time.

For more information about this article, please visit the publication web page here: https://pubs.acs.org/doi/10.1021/acs.analchem.1c02199.

If you would like to learn more about glyXera’s high-performance xCGE-LIF technology and its applications in the characterization of glycoproteins and biopharmaceuticals, please don’t hesitate to get in touch with us.