Unveiling Membrane Proteins at the Nanoscale: Mass Spectrometry from Recombinant Complexes to Brain Regions

In 2008, a groundbreaking milestone was achieved when scientists captured the first mass spectra of intact membrane protein complexes, detached from their native detergent micelles, directly in the gas phase. This achievement opened a new frontier in nanoscience, allowing detailed investigation of the molecular architecture and dynamics of these elusive, membrane-embedded entities.

Harnessing advanced mass spectrometry techniques, researchers can now probe the structural integrity, lipid interactions, and functional states of complex membrane proteins such as rotary ATPases, G-protein coupled receptors (GPCRs), ABC transporters, ion channels, and solute carriers??"all at the nanoscale. These insights are crucial for understanding how lipids and drugs modulate transport, coupling mechanisms, and signal transduction within the membrane environment.

The implications are profound for drug discovery: mass spectrometry enables high-resolution ligand screening for GPCRs, ion channels, and transporters directly from native membranes. Recent innovations push this approach further, allowing the extraction and analysis of membrane proteins directly from tissues??"such as specific brain regions implicated in psychiatric disorders??"providing a window into the molecular underpinnings of neurobiology at the nanoscale.

I will highlight recent case studies demonstrating how this nanoscale perspective is transforming our understanding of membrane protein function and paving the way for targeted therapeutics.

Speaker: Carol Robinson, Oxford University

Editor's Note: Two lectures are scheduled for this date and time in the same room.  One is most likely being held on a different date.