Towards structural glycoproteomics
The majority of human proteins are decorated with complex polysaccharides, called glycans, that play key roles in protein biology. Seemingly subtle changes in the structural configuration of glycans can severely impact protein functionality and biological processes. The non-template driven enzymatic glycan synthesis pathway is capable of producing a myriad of unique glycans. Already in healthy individuals, the diversity and stoichiometry of glycans on proteins can vastly differ in a tissue-, protein-, and site-specific manner. Protein glycosylation is also very dynamic since many different factors can influence glycan synthesis steps, as is painfully demonstrated in congenital disorders of glycosylation. For both genetic and acquired human disease, glycobiology offers unique clinical utility for biomarker applications, drug target discovery, and design of rational treatment strategies.
The key to unlock the true potential of glycobiology for healthcare innovations lies within analytical capabilities to decipher the sugar code on glycoproteins. At present, analysis of glycopeptides from enzymatic protein digests is increasingly used to define glycan repertoire changes on proteins at glycosylation site resolution between conditions. It enabled biomarker discovery, diagnostic applications, and novel insights in protein glycobiology. Nevertheless, glycopeptide profiling is typically unable to resolve the fine structural or even topological features of glycan-moieties. This limitation makes the interpretation of results challenging and may lead to incorrect conclusions since glycan trees are typically inferred from just sugar compositions. It is therefore paramount to move towards structural glycoproteomics by resolving this bottleneck through combined hardware, software, and method development.
Key Learning Objectives
- Updated glycoproteomics workflows
- Glycoproteomics for translational research
- From glycopeptide profiling to structural insights
- How real-tims bioinformatics can be used there
- timsOmni™, Glyco-PASEF® & Myriad
Who Should Attend
- Translational biology researchers
- Proteomics researchers and core facility managers
- Structural (glyco) protein researchers
- Proteomics bioinformaticians
- Biomarker discovery researchers
Presenter: Hans Wessels, Ph.D., Glycoproteomics Scientist, Radboudumc, Nijmegen, Netherlands
Dr. Hans Wessels has been working in the field of MS-based proteomics since more than 20 years now. He got his Ph.D. in mitochondrial proteomics from Radboud University Nijmegen and has developed deep expertise in analytical biochemistry, glycobiology, and translational research.
He is now is a Proteomics Scientist and Director of the Radboud Technology Center for Mass Spectrometry at the Radboud University Medical Center (RUMC) in Nijmegen, The Netherlands. His work is embedded within the Translational Metabolic Laboratory, Department of Human Genetics, where he focuses on disease-specific proteoforms, glycoproteomics, and advanced mass spectrometry workflows.
He has developed deep expertise in analytical biochemistry, glycobiology, and translational research. His research combines cutting-edge PASEF-based mass spectrometry, real-time search strategies, and bioinformatics to advance biomarker discovery and clinical applications.
Dr. Wessels is an active contributor to collaborative initiatives including the Radboud Consortium for Glycoscience, the X-omics Initiative, and the EnFORCE project, and frequently engages in scientific dissemination through webinars and international collaborations.
