MASSive CASA – Thursday 25th of August (9:30 – 17:00h)

On Thursday 25/08 we are organizing a 1-day CASA symposium on Mass Spectrometry with Mike Gross and Ljiljana Paša-Tolić as our main guests and with a great supporting act by our CASA-IMSC2022 presenters as a final practice round for the upcoming IMSC2022 conference.

Below you can find the program for our exciting live event between VU and UvA!

Morning program – Auditorium (00E70) – O|2 Lab Building, VU Amsterdam

9:30-10:30 IMSC2022 preparation session I

9:30-9:47 Ziran Zhai (UvA) -Comparison of hydrophilic interaction chromatography and native size-exclusion chromatography mass spectrometry for the characterization of heavily glycated proteins

9:50-10:07 Peng Che (VU Amsterdam) – A “chemical toolbox” for the generation of metabolite-like products of new psychoactive substances
10:10-10:20 Annika van der Zon (UvA) – Acrylamide Monoliths for Hydrophilic Interaction Liquid Chromatography-Mass Spectrometry of Intact (Glyco)proteins (student pitch)

10:20-10:30 discussion with speakers

10:30-11:00 coffee  

11:00-11:45 BAC seminar key note:

Prof. Michael L Gross (Washington University in St Louis, USA)

Protein Footprinting: A Unique Source of Structural Information
Unlike most spectroscopic and thermodynamic information sources about protein structure and interactions, mass spectrometry-based proteomics provides a much deeper insight at the regional or peptide level and even at the amino acid level. Among these approaches, termed protein footprinting, are hydrogen/deuterium exchange and free radical labeling via a “fast photochemical oxidation of proteins” or FPOP. These approaches can afford a structural view of protein folding, interactions with metal ions, protein aggregation (especially of amyloid proteins), and membrane proteins. Advantages of FPOP are its speed, broad coverage, and irreversible changes imparted on the protein. We will provide a brief description of methodology followed by examples of problem solving in protein structure.

 

11:45-13:45 Time for lunch & transfer to UvA

 

Afternoon program – C0.05, Science Park 904, UvA (chair/host: Andrea Gargano)

13:45-15:00 IMSC2022 preparation session II


13:45-14:02 Agathe Depraz Depland (VU Amsterdam) – Unravelling the peptides’ aggregation mechanism: The challenge of IM-MS instrumentation to probe heterogeneous and fragile processes

14:05-14:22 Wouter Knol (UvA) – Sequence determination of copolymers by mass spectrometry after pyrolysis-gas chromatography

14:25-14:42 Melissa Bärenfänger (VU Amsterdam) – Establishing structural MS to understand protein glycosylation in neurological function and disease

14:45-15:00 discussion with speakers

15:00-15:30 coffee

15:30-16:15 John van Geuns Lecture


Dr. Ljiljana Paša-Tolić (Pacific Northwest National Laboratory, USA)

Recent advances in spatial and cellular proteomics and multiomics

Spatial molecular profiling (omics) provides invaluable information on structural organization and cell-to-cell interactions in native tissues, organs, and communities. Development and rapid dissemination of single-cell DNA and RNA sequencing have dramatically advanced our understanding of cellular diversity and heterogeneity. However, these technologies capture only a partial picture of a cell’s phenotype. Proteins and proteoforms are of particular interest in establishing cellular identities because they are the primary effectors of biological function, and their modification state or abundance cannot be easily inferred from mRNA measurements. However, the ability to measure proteins and proteoforms in a few cells or a single cell is a major analytical challenge.
Current approaches for probing spatial distribution of the proteome typically rely on the use of labels or antibodies, which limits multiplexing and requires a priori knowledge of protein targets. Conventional bottom-up proteomics in nanoPOTS format has been recently demonstrated for proteome-wide analysis of small tissue sections. However, this approach cannot provide proteoform maps and is therefore lacking because proteoforms drive cellular functions. To address the proteoform mapping challenge with enhanced throughput and resolution, we integrated nanoPOTS top-down proteomics and MALDI mass spectrometry imaging. In this presentation we will demonstrate how advanced FTMS instrumentation and methods can map proteoforms in human organs at near single cell resolution. We will also briefly discuss exciting new developments allowing for multimodal profiling of thousands of mRNA transcripts and proteins from the same single-cells and identification of cell-type-specific markers in both modalities.

16:15 IMSC2022 Posters & Get together with drinks!

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