March 5-9, 2022
Georgia World Congress Center
Atlanta, Georgia, USA

Wallace H. Coulter Lecture
New Horizons in Mass Spectrometry; Sizing and Counting Particles by Native Mass Spectrometry

Lecture Details

Monday, March 7
5:00 PM
Sidney Marcus Auditorium
Presented by Professor Albert J.R. Heck
Science Faculty of Utrecht University

High-resolution native mass spectrometry enables the mass analysis of intact proteins and protein assemblies, ranging from antibodies to naïve viruses with molecular weights beyond 10 MDa. In this lecture recent advances in this field will be highlighted, including extending the attainable mass range, the sensitivity of detection, the mass resolving power and the proteoform specificity.

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Abstract: New Horizons in Mass Spectrometry; Sizing and Counting Particles by Native Mass Spectrometry

High-resolution native mass spectrometry enables the mass analysis of intact proteins and protein assemblies, ranging from antibodies to naïve viruses with molecular weights beyond 10 MDa. In this lecture recent advances in this field will be highlighted, including extending the attainable mass range, the sensitivity of detection, the mass resolving power and the proteoform specificity.

Cumulatively, these advances have initiated new applications, not only in the detailed characterization of advanced biopharmaceuticals, but also in analysis of the plasma (glyco)proteome and the analysis of very large heterogeneous assemblies.

Modern mass analyzers are sufficiently sensitive to detect single molecules by charge detection mass spectrometry, enabling the analysis by native MS of very large heterogeneous assemblies like plasma immunoglobulins, proteaceous nanocontainers, SARS-Cov2 spike protein-antibody immune-complexes, viruses, and virus-based gene-delivery vectors.

Advanced biopharmaceuticals as well as serum glycoproteins are characterized by a plethora of proteoform, due to glycosylation and phosphorylation. High-resolution native MS can be used for comprehensive proteoform profiling. Unlike most clinical assays, this approach enables the monitoring of not only protein abundance, but also proteoform abundance, allowing us to address an intriguing question; How unique and personalized is our serum proteome?

These advances illustrate the broad impact of native MS in various disciplines of the life sciences.

Lecture Philosophy
Pittcon and the Wallace H. Coulter Foundation promote educational training and development in laboratory sciences, with special emphasis in resource limited countries worldwide.

The lecture features an outstanding individual who has demonstrated a lifetime commitment to, and made important contributions that have had a significant impact on education, practice and/or research in laboratory science.

Who is Professor Albert Heck?

Albert J. R. Heck (1964) is distinguished faculty professor at the Science Faculty of Utrecht University (The Netherlands). 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 stable-isotope-labeling, the use of alternative proteases and hybrid peptide- and protein-centric fragmentation techniques. Heck is also known for his expertise in structural biology, being a pioneer in native- and cross-linking mass spectrometry, and glycoproteomics.

Heck has been coordinating several national and EU-funded large-scale proteomics facilities, such as the Netherlands Proteomics Center and Prime-XS. 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). He is member of the Royal Netherlands Academy of Sciences and Arts and EMBO.

 

 

 

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