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Desorption Electrospray Ionization Mass Spectrometry Imaging of Proteins Directly from Biological Tissue Sections
Author(s) -
Kyana Y. Garza,
Clara L. Feider,
Dustin R. Klein,
Jake Rosenberg,
Jennifer S. Brodbelt,
Lívia S. Eberlin
Publication year - 2018
Publication title -
analytical chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.117
H-Index - 332
eISSN - 1520-6882
pISSN - 0003-2700
DOI - 10.1021/acs.analchem.8b00967
Subject(s) - chemistry , desorption electrospray ionization , biomolecule , mass spectrometry , mass spectrometry imaging , biological tissue , ionization , electrospray ionization , ion mobility spectrometry , fragmentation (computing) , dissociation (chemistry) , electrospray , top down proteomics , analytical chemistry (journal) , chromatography , protein mass spectrometry , ion , chemical ionization , biochemistry , biomedical engineering , medicine , organic chemistry , computer science , operating system
Analysis of large biomolecules including proteins has proven challenging using ambient ionization mass spectrometry imaging techniques. Here, we have successfully optimized desorption electrospray ionization mass spectrometry (DESI-MS) to detect intact proteins directly from tissue sections and further integrated DESI-MS to a high field asymmetric waveform ion mobility (FAIMS) device for protein imaging. Optimized DESI-FAIMS-MS parameters were used to image mouse kidney, mouse brain, and human ovarian and breast tissue samples, allowing detection of 11, 16, 14, and 16 proteoforms, respectively. Identification of protein species detected by DESI-MS was performed on-tissue by top-down ultraviolet photodissociation (UVPD) and collision induced dissociation (CID) as well as using tissue extracts by bottom-up CID and top-down UVPD. Our results demonstrate that DESI-MS imaging is suitable for the analysis of the distribution of proteins within biological tissue sections.

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