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Comprehensive LESA Mass Spectrometry Imaging of Intact Proteins by Integration of Cylindrical FAIMS.
Anal Chem 2020AC

Abstract

The 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.

Authors+Show Affiliations

School of Biosciences , University of Birmingham , Edgbaston , Birmingham B15 2TT , United Kingdom.School of Biosciences , University of Birmingham , Edgbaston , Birmingham B15 2TT , United Kingdom. EPSRC Centre for Doctoral Training in Physical Sciences for Health , University of Birmingham , Birmingham B15 2TT , United Kingdom.Thermo Fisher Scientific , Memorial Drive , Cambridge , Massachusetts 02139 , United States.Thermo Fisher Scientific , River Oaks Parkway , San Jose , California 95134 , United States.School of Computer Sciences , University of Birmingham , Birmingham B15 2TT , United Kingdom.School of Biosciences , University of Birmingham , Edgbaston , Birmingham B15 2TT , United Kingdom.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31967787

Citation

Griffiths, Rian L., et al. "Comprehensive LESA Mass Spectrometry Imaging of Intact Proteins By Integration of Cylindrical FAIMS." Analytical Chemistry, 2020.
Griffiths RL, Hughes JW, Abbatiello SE, et al. Comprehensive LESA Mass Spectrometry Imaging of Intact Proteins by Integration of Cylindrical FAIMS. Anal Chem. 2020.
Griffiths, R. L., Hughes, J. W., Abbatiello, S. E., Belford, M. W., Styles, I. B., & Cooper, H. J. (2020). Comprehensive LESA Mass Spectrometry Imaging of Intact Proteins by Integration of Cylindrical FAIMS. Analytical Chemistry, doi:10.1021/acs.analchem.9b05124.
Griffiths RL, et al. Comprehensive LESA Mass Spectrometry Imaging of Intact Proteins By Integration of Cylindrical FAIMS. Anal Chem. 2020 Jan 28; PubMed PMID: 31967787.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Comprehensive LESA Mass Spectrometry Imaging of Intact Proteins by Integration of Cylindrical FAIMS. AU - Griffiths,Rian L, AU - Hughes,James W, AU - Abbatiello,Susan E, AU - Belford,Michael W, AU - Styles,Iain B, AU - Cooper,Helen J, Y1 - 2020/01/28/ PY - 2020/1/23/pubmed PY - 2020/1/23/medline PY - 2020/1/23/entrez JF - Analytical chemistry JO - Anal. Chem. N2 - The 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. SN - 1520-6882 UR - https://www.unboundmedicine.com/medline/citation/31967787/Comprehensive_LESA_mass_spectrometry_imaging_of_intact_proteins_by_integration_of_cylindrical_FAIMS L2 - https://dx.doi.org/10.1021/acs.analchem.9b05124 DB - PRIME DP - Unbound Medicine ER -