Journal
ANALYTICAL CHEMISTRY
Volume 85, Issue 15, Pages 7191-7196Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac400902h
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Funding
- National Institute of General Medical Sciences [5 P41 GM103391-02]
- National Center for Research Resources [5P41RR031461-01]
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Transmembrane proteins are greatly under-represented in data generated by imaging mass spectrometry (IMS) because of analytical challenges related to their size and solubility. Here, we present the first example of MALDI IMS of two highly modified multitransmembrane domain proteins, myelin proteolipid protein (PLP, 30 kDa) and DM-20 (26 kDa), from various regions of rat brain, namely, the cerebrum, cerebellum, and medulla. We utilize a novel tissue pretreatment aimed at transmembrane protein enrichment to show the in situ distribution of fatty acylation of these proteins, particularly of post-translational palmitoylation. Additionally, we demonstrate the utility of protease-encapsulated hydrogels for spatially localized on-tissue protein digestion and peptide extraction for subsequent direct coupling to LC-MS/MS for protein identification.
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