Lecture
Native ambient mass spectrometry imaging of proteins and their complexes: Latest developments and applications
- at -
- ICM Saal 4b
- Type: Lecture
Lecture description
Helen J. Cooper1,2, Oliver J. Hale1,2, Sarah Vickers1, Cameron Baines1, Jack R. Roberts2 and Tin Yi Lui2
1School of Biosciences, University of Birmingham / 2Rosalind Franklin Institute, Rutherford Appleton Laboratory
Native ambient mass spectrometry (NAMS) combines native mass spectrometry, an established technique in structural biology, and ambient mass spectrometry, in which biological substrates such as thin tissue sections are analysed directly with little or no sample preparation. The combined benefits of NAMS for analysis of protein assemblies and protein-ligand complexes include measurement of accurate mass and stoichiometry, identification of both protein and non-covalently bound ligands, together with information on spatial distribution. Recent efforts using nanospray desorption electrospray ionization (nano-DESI), have advanced NAMS for the analysis of fresh frozen issue, allowing the spatial distribution of protein assemblies to be mapped. Endogenous protein assemblies and their constituents (including small molecule ligands) can be identified by top-down dissection of assemblies in the gas phase, potentially allowing the discovery of new protein-ligand interactions.
In this presentation, recent developments in native ambient mass spectrometry imaging will be discussed, including approaches for the analysis of integral membrane proteins and membrane-associated proteins, improvements in sensitivity and accessible molecular weight, and applications in drug discovery and molecular pathology associated with neurodegenerative diseases.
1School of Biosciences, University of Birmingham / 2Rosalind Franklin Institute, Rutherford Appleton Laboratory
Native ambient mass spectrometry (NAMS) combines native mass spectrometry, an established technique in structural biology, and ambient mass spectrometry, in which biological substrates such as thin tissue sections are analysed directly with little or no sample preparation. The combined benefits of NAMS for analysis of protein assemblies and protein-ligand complexes include measurement of accurate mass and stoichiometry, identification of both protein and non-covalently bound ligands, together with information on spatial distribution. Recent efforts using nanospray desorption electrospray ionization (nano-DESI), have advanced NAMS for the analysis of fresh frozen issue, allowing the spatial distribution of protein assemblies to be mapped. Endogenous protein assemblies and their constituents (including small molecule ligands) can be identified by top-down dissection of assemblies in the gas phase, potentially allowing the discovery of new protein-ligand interactions.
In this presentation, recent developments in native ambient mass spectrometry imaging will be discussed, including approaches for the analysis of integral membrane proteins and membrane-associated proteins, improvements in sensitivity and accessible molecular weight, and applications in drug discovery and molecular pathology associated with neurodegenerative diseases.
