title: FTIR imaging of the molecular burden around Aβ deposits in an early-stage 3-Tg-APP-PSP1-TAU mouse model of Alzheimer's disease.
abstract: Alzheimer's disease is one of the major causes of dementia in the elderly. The disease is caused by the misfolding of water soluble alpha-helical proteins, which leads to the accumulation of β-sheets in the form of amyloid plaques, which can subsequently affect surrounding tissue areas by oxidative stress neurotoxicity. The aim of the present study was to design a novel methodology to analyze the extent to the neuronal burden around protein-rich Aβ plaques suspected to affect molecular components by oxidative stress induced by inflammatory states. To do so, sagittal brain tissue sections from triple transgenic APPxPSP1xTAU mice were used to carry high magnification FTIR-FPA bench-top chemical imaging. The study used the combination of chemometric procedures involving spectral curve fitting and image processing to study the molecular changes occurring around the plaques. The study shows the performance of the approach by demonstrating its usefulness to co-localize molecular changes to different areas around the plaques. The results, although very preliminary, point to the strong interplay between the distance from the plaque and co-accumulation of molecular components indicative of inflammatory states.
authors.affiliation: AGH University of Science and Technology, Faculty of Physics and Applied Computer Science, Krakow, Poland.
authors.forename: Artur Dawid
authors.initials: AD
authors.lastname: Surowka
authors.affiliation: Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, UK. peter.gardner@manchester.ac.uk and School of Chemical Engineering and Analytical Science, University of Manchester, Oxford Road, Manchester, UK.
authors.forename: Michael
authors.identifier: 0000-0003-1634-3326
authors.initials: M
authors.lastname: Pilling
authors.affiliation: Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, UK. peter.gardner@manchester.ac.uk and School of Chemical Engineering and Analytical Science, University of Manchester, Oxford Road, Manchester, UK.
authors.forename: Alex
authors.identifier: 0000-0002-5791-8555
authors.initials: A
authors.lastname: Henderson
authors.affiliation: Wolfson Molecular Imaging Centre, University of Manchester, Manchester, UK.
authors.forename: Herve
authors.initials: H
authors.lastname: Boutin
authors.affiliation: Wolfson Molecular Imaging Centre, University of Manchester, Manchester, UK.
authors.forename: Lidan
authors.initials: L
authors.lastname: Christie
authors.affiliation: AGH University of Science and Technology, Faculty of Physics and Applied Computer Science, Krakow, Poland.
authors.forename: Magdalena
authors.initials: M
authors.lastname: Szczerbowska-Boruchowska
authors.affiliation: Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, UK. peter.gardner@manchester.ac.uk and School of Chemical Engineering and Analytical Science, University of Manchester, Oxford Road, Manchester, UK.
authors.forename: Peter
authors.identifier: 0000-0003-4034-3764
authors.initials: P
authors.lastname: Gardner
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D004195:Disease Models, Animal; D051379:Mice; D008822:Mice, Transgenic; D057054:Molecular Imaging / Q000379:methods*; D000072757:Protein Conformation, beta-Strand; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D016229:Amyloid beta-Peptides