TY - JOUR
T1 - From mouse to human
T2 - Comparative analysis between grey and white matter by synchrotron-fourier transformed infrared microspectroscopy
AU - Sanchez-Molina, Paula
AU - Valente, Tony
AU - Almolda, Beatriz
AU - González, Berta
AU - Castellano, Bernardo
AU - Perálvarez-Marín, Alex
AU - Kreuzer, Martin
AU - Benseny-Cases, Núria
N1 - Funding Information:
Funding: This work was supported by the Spanish Ministry of Economy and Business through Plan Estatal BFU2017-87843-R to A.P.-M. and B.C.
Publisher Copyright:
© 2020 by the authors. Licensee MDPI, Basel, Switzerland.
Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 2020/8
Y1 - 2020/8
N2 - Fourier Transform Infrared microspectroscopy (µFTIR) is a very useful method to analyze the biochemical properties of biological samples in situ. Many diseases affecting the central nervous system (CNS) have been studied using this method, to elucidate alterations in lipid oxidation or protein aggregation, among others. In this work, we describe in detail the characteristics between grey matter (GM) and white matter (WM) areas of the human brain by µFTIR, and we compare them with the mouse brain (strain C57BL/6), the most used animal model in neurological disorders. Our results show a clear different infrared profile between brain areas in the lipid region of both species. After applying a second derivative in the data, we established a 1.5 threshold value for the lipid/protein ratio to discriminate between GM and WM areas in non-pathological conditions. Furthermore, we demonstrated intrinsic differences of lipids and proteins by cerebral area. Lipids from GM present higher C=CH, C=O and CH3 functional groups compared to WM in humans and mice. Regarding proteins, GM present lower Amide II amounts and higher intramolecular β-sheet structure amounts with respect to WM in both species. However, the presence of intermolecular β-sheet structures, which is related to β-aggregation, was only observed in the GM of some human individuals. The present study defines the relevant biochemical properties of non-pathological human and mouse brains by µFTIR as a benchmark for future studies involving CNS pathological samples.
AB - Fourier Transform Infrared microspectroscopy (µFTIR) is a very useful method to analyze the biochemical properties of biological samples in situ. Many diseases affecting the central nervous system (CNS) have been studied using this method, to elucidate alterations in lipid oxidation or protein aggregation, among others. In this work, we describe in detail the characteristics between grey matter (GM) and white matter (WM) areas of the human brain by µFTIR, and we compare them with the mouse brain (strain C57BL/6), the most used animal model in neurological disorders. Our results show a clear different infrared profile between brain areas in the lipid region of both species. After applying a second derivative in the data, we established a 1.5 threshold value for the lipid/protein ratio to discriminate between GM and WM areas in non-pathological conditions. Furthermore, we demonstrated intrinsic differences of lipids and proteins by cerebral area. Lipids from GM present higher C=CH, C=O and CH3 functional groups compared to WM in humans and mice. Regarding proteins, GM present lower Amide II amounts and higher intramolecular β-sheet structure amounts with respect to WM in both species. However, the presence of intermolecular β-sheet structures, which is related to β-aggregation, was only observed in the GM of some human individuals. The present study defines the relevant biochemical properties of non-pathological human and mouse brains by µFTIR as a benchmark for future studies involving CNS pathological samples.
KW - Central nervous system
KW - Grey matter
KW - Infrared spectroscopy
KW - Lipid oxidation
KW - Protein structure
KW - White matter
UR - http://www.scopus.com/inward/record.url?scp=85088565079&partnerID=8YFLogxK
U2 - 10.3390/biom10081099
DO - 10.3390/biom10081099
M3 - Artículo
C2 - 32722088
AN - SCOPUS:85088565079
SN - 2218-273X
VL - 10
SP - 1
EP - 14
JO - Biomolecules
JF - Biomolecules
IS - 8
M1 - 1099
ER -
