A Detailed Look at Antibodies, Plasma Proteins, Viruses and Gene-Delivery Vehicles by High-Resolution Native Mass Spectrometry
Modern biopharmaceutical products, and most plasma proteins, exhibit extensive structural micro-heterogeneity due to co-occurring post-translational modifications. These modifications affect their functionality and thus need to be characterized in detail. We use high-resolution native mass spectrometry, often combined with glycoproteomics and top- and middle-down proteomics, to analyze this micro-heterogeneity. Taking mAbs, erythropoietin and plasma proteins as model systems, we demonstrate an all-inclusive quantitative profiling of glycoproteins. We demonstrate the usage of a biosimilarity score to quantitatively assess structural similarities.
Moreover, by extending the mass range of Orbitrap mass analyzers we have expanded the reach of native mass spectrometry to higher molecular weight compounds, such as IgG hexamers, endogenous viruses and gene delivery vectors such as the adenovirus. Professor Albert Heck will describe the latest developments, including Orbitrap-based single particle charge detection mass spectrometry, and how that can be used to assess the quality and purity of this next generation of biopharmaceutical products.
Key learning objectives:
- Learn about ways to analyze next generation of biopharmaceutical products with different MS methods
- See methods developed to analyze IgG hexamers, endogenous viruses and adenovirus delivery vectors
- Native mass spectrometry strategies for the analysis of higher molecular weight compounds
Who should attend:
- Biopharmaceutical Research Scientists
- Analytical Scientists from Biopharma companies working on or interested in gene therapy analysis
- PhD students in any field of biotherapeutic drug development
- Scientists looking to advance knowledge of gene therapy
Presenter: Professor Albert J.R. Heck (Distinguished Faculty Professor, Utrecht University)
Albert J. R. Heck (1964) is distinguished faculty professor at Utrecht University (NL), chair of the Biomolecular Mass Spectrometry and Proteomics group. His research focuses on the development and applications of mass spectrometry-based proteomics and structural biology. Heck introduced innovative proteomics technologies for phospho-enrichment, the use of alternative proteases and hybrid peptide fragmentation techniques. Heck is also known for his expertise in structural biology, being a pioneer in native- and cross-linking mass spectrometry. Heck has been coordinating several national and EU-funded large-scale proteomics facilities. Heck is recipient of numerous awards including the Field and Franklin Award (ACS), The Thomson Medal (IMSF), the Krebs Medal (FEBS) and Spinoza Award (NWO). Recently, his research has focused on using mass spectrometry to characterize plasma proteins and perform plasma proteomics, including the analysis of human immunoglobulin repertoires.
