Hydrogen Exchange-Mass Spectrometry for Analysis of Higher-Order Structure of Protein Therapeutics Across the Pipeline
Over the past three decades, hydrogen exchange-mass spectrometry (HX-MS) has advanced from an esoteric research tool to a highly repeatable analytical method sensitive to subtle changes in the higher-order structure of proteins. The method is now widely employed in drug discovery and vaccine development for the mapping of conformational epitopes. More recent work suggests that HX-MS data has the potential to also support process and analytical development as well as provide information for regulatory considerations. In this webinar, Dr. David Weis, Professor of Chemistry at University of Kansas, will provide a brief overview of what is measured in HX-MS and how results are interpreted. Weis will also cover the:
Broad characterization of the epitopic surface of ricin toxin
Mapping effects of preservatives and other excipients on aggregation hotspots
Mapping sites of reversible self-association
Development of an analytical framework to evaluate structural similarity of therapeutic proteins
Key Learning Objectives:
- Fundamentals of HX
- Measurement of HX by MS
- Applications of HX for therapeutic proteins
Who Should Attend:
- Scientists engaged with characterization of higher-order structure of protein complexes, including:
- Biopharma discovery, process development and characterization
- Academia, biophysics, pharmacy, top-down proteomics, proteoform ID