Native mass spectrometry seeks to
probe noncovalent protein interactions
in terms of protein quaternary structure, protein–protein and
protein–ligand complexes. The ultimate goal is to link the
understanding of protein interactions to the protein environment by
visualizing the spatial distribution of noncovalent protein interactions
within tissue. Previously, we have shown that noncovalently bound
protein complexes can be directly probed via liquid extraction surface
analysis from dried blood spot samples, where hemoglobin is highly
abundant. Here, we show that the intact hemoglobin complex can be
sampled directly from thin tissue sections of mouse liver and correlated
to a visible vascular feature, paving the way for native mass spectrometry
imaging