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Comprehensive LESA Mass Spectrometry Imaging of Intact Proteins by Integration of Cylindrical FAIMS
dataset
posted on 2020-01-28, 12:33 authored by Rian L. Griffiths, James W. Hughes, Susan E. Abbatiello, Michael W. Belford, Iain B. Styles, Helen J. CooperThe
benefits of high field asymmetric waveform ion mobility spectrometry
(FAIMS) for mass spectrometry imaging of intact proteins in thin tissue
sections have been demonstrated previously. In those works, a planar
FAIMS device coupled with a Thermo Elite mass spectrometer was employed.
Here, we have evaluated a newly introduced cylindrical FAIMS device
(the FAIMS Pro) coupled with a Thermo Fusion Lumos mass spectrometer
for liquid extraction surface analysis mass spectrometry imaging of
intact proteins in thin tissue sections from rat testes, kidney, and
brain. The method makes use of multiple FAIMS compensation values
at each location (pixel) of the imaging array. A total of 975 nonredundant
protein species were detected in the testes imaging dataset, 981 in
the kidney dataset, and 249 in the brain dataset. These numbers represent
a 7-fold (brain) and over 10-fold (testes, kidney) improvement on
the numbers of proteins previously detected in LESA FAIMS imaging,
and a 10-fold to over 20-fold improvement on the numbers detected
without FAIMS on this higher performance mass spectrometer, approaching
the same order of magnitude as those obtained in top-down proteomics
of cell lines. Nevertheless, high throughput identification within
the LESA FAIMS imaging workflow remains a challenge.
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Comprehensive LESA Mass Spectrometry Imagingtestes imaging datasetmass spectrometry imagingFAIMS compensation values975 nonredundant protein speciesperformance mass spectrometerLESA FAIMS imaging workflowLESA FAIMS imagingextraction surface analysis mass spectrometry imagingThermo Elite mass spectrometerThermo Fusion Lumos mass spectrometerwaveform ion mobility spectrometrytissue sectionsFAIMS device