title: LESA FAIMS Mass Spectrometry for the Spatial Profiling of Proteins from Tissue.
abstract: We have shown previously that coupling of high field asymmetric waveform ion mobility spectrometry (FAIMS), also known as differential ion mobility, with liquid extraction surface analysis (LESA) mass spectrometry of tissue results in significant improvements in the resulting protein mass spectra. Here, we demonstrate LESA FAIMS mass spectrometry imaging of proteins in sections of mouse brain and liver tissue. The results are compared with LESA mass spectrometry images obtained in the absence of FAIMS. The results show that the number of different protein species detected can be significantly increased by incorporating FAIMS into the workflow. A total of 34 proteins were detected by LESA FAIMS mass spectrometry imaging of mouse brain, of which 26 were unique to FAIMS, compared with 15 proteins (7 unique) detected by LESA mass spectrometry imaging. A number of proteins were identified including α-globin, 6.8 kDa mitochondrial proteolipid, macrophage migration inhibitory factor, ubiquitin, β-thymosin 4, and calmodulin. A total of 40 species were detected by LESA FAIMS mass spectrometry imaging of mouse liver, of which 29 were unique to FAIMS, compared with 24 proteins (13 unique) detected by LESA mass spectrometry imaging. The spatial distributions of proteins identified in both LESA mass spectrometry imaging and LESA FAIMS mass spectrometry imaging were in good agreement indicating that FAIMS is a suitable tool for inclusion in mass spectrometry imaging workflows.
authors.affiliation: School of Biosciences, University of Birmingham , Edgbaston, Birmingham B15 2TT, U.K.
authors.forename: Rian L
authors.initials: RL
authors.lastname: Griffiths
authors.affiliation: School of Biosciences, University of Birmingham , Edgbaston, Birmingham B15 2TT, U.K.
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Creese
authors.affiliation: National Physical Laboratory , Hampton Road, Teddington, Middlesex, TW11 0LW, U.K.
authors.forename: Alan M
authors.initials: AM
authors.lastname: Race
authors.affiliation: National Physical Laboratory , Hampton Road, Teddington, Middlesex, TW11 0LW, U.K.|School of Pharmacy, University of Nottingham , University Park, Nottingham NG7 2RD, U.K.
authors.forename: Josephine
authors.initials: J
authors.lastname: Bunch
authors.affiliation: School of Biosciences, University of Birmingham , Edgbaston, Birmingham B15 2TT, U.K.
authors.forename: Helen J
authors.initials: HJ
authors.lastname: Cooper
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000378:metabolism* / Q000473:pathology; D000075663:Ion Mobility Spectrometry; D008099:Liver / Q000378:metabolism* / Q000473:pathology; D013058:Mass Spectrometry / Q000379:methods*; D051379:Mice; D011506:Proteins / Q000032:analysis*
chemical_list: D011506:Proteins