Analytical and Informatic Tools to Explore the Glycoproteome

Haley M. Schramm (1), Tim S. Veth (1), Kathryn Kothlow (1), Joshua D. Hinkle (2), Jingjing Huang (2), David Bergen (2), Rafael D. Melani (2), Graeme C. McAlister (2), Christopher Mullen (2), and Nicholas M. Riley (1)
(1) Department of Chemistry, University of Washington, Seattle, WA, USA (2) Thermo Fisher Scientific, San Jose, CA, USA 

Nicholas Riley, PhD (Presenter) University of Washington

Presenter Bio: I am an assistant professor in the Department of Chemistry at the University of Washington. I am originally from Louisville, KY and I earned my B.S. from the University of South Carolina. I did my graduate studies at UW-Madison in Josh Coon's group, where I worked on mass spectrometry instrumentation, electron transfer dissociation technologies, and proteomics methodology. I then moved to Stanford University for my postdoc in Carolyn Bertozzi's group, where I worked on glycoproteomics and chemical glycobiology. I started my independent group at UW in fall 2023, and we focus on building technologies for investigating glycoproteome regulation. One of our big goals is to understand the molecular details of how altered cell surface phenotypes manifest in cancer progression and drive metastasis.

Relevant Financial Disclosures (within past 24 months, reported on Jun 26, 2026) No relevant financial relationship(s) to disclose.

Glycopeptide tandem MS spectra are complex and often challenging to interpret, even with modern search engines that have significantly improved the ability to assign glycopeptide identifications. Here I will discuss several strategies our group is developing to help glycoproteomics data analysis, both before and after glycopeptides are identified through database searches. I will also highlight several examples of how these tools have subsequently helped us refine the methods we use to interrogate glycoproteoforms, including using ion-ion reactions like electron transfer dissociation and proton transfer charge reduction to characterize glycopeptides and intact glycoproteins.