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Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients.

Araki K, Yagi N, Ikemoto Y, Yagi H, Choong CJ, Hayakawa H, Beck G, Sumi H, Fujimura H, Moriwaki T, Nagai Y, Goto Y, Mochizuki H - Sci Rep (2015)

Bottom Line: Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients.Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs.Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

ABSTRACT
Lewy bodies (LBs), which mainly consist of α-synuclein (α-syn), are neuropathological hallmarks of patients with Parkinson's disease (PD). The fine structure of LBs is unknown, and LBs cannot be made artificially. Nevertheless, many studies have described fibrillisation using recombinant α-syn purified from E. coli. An extremely fundamental problem is whether the structure of LBs is the same as that of recombinant amyloid fibrils. Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients. Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs. Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.

No MeSH data available.


Related in: MedlinePlus

The solid black line in each panel shows an FTIRM spectrum (amide I region) obtained from (A) fibrils of α-syn expressed in E. coli, (B) normal brain tissue from the patient with AD, (C) the core of an SP, (D) normal brain tissue from the brain of the patient with PD, (E) the core of an LB, and (F) the halo of an LB.Blue and red lines represent contributions of β-sheet structures and non-β-sheet structures (random coils, α-helices, and others), respectively. The dotted line represents the fitted curve. Data were fitted using a Gaussian species model centred at 1628, 1680 (β-sheets, blue line), 1648, and 1661 (random coils, α-helices, and others, red line) cm−1 123031.
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f3: The solid black line in each panel shows an FTIRM spectrum (amide I region) obtained from (A) fibrils of α-syn expressed in E. coli, (B) normal brain tissue from the patient with AD, (C) the core of an SP, (D) normal brain tissue from the brain of the patient with PD, (E) the core of an LB, and (F) the halo of an LB.Blue and red lines represent contributions of β-sheet structures and non-β-sheet structures (random coils, α-helices, and others), respectively. The dotted line represents the fitted curve. Data were fitted using a Gaussian species model centred at 1628, 1680 (β-sheets, blue line), 1648, and 1661 (random coils, α-helices, and others, red line) cm−1 123031.

Mentions: Figure 3 shows the FTIR spectra of recombinant α-syn fibrils (A), of brain sections from an SP of an Alzheimer’s disease (AD) patient (Fig. 3B,C), and of an LB of an 83-year-old female PD patient (Fig. 3D–F). The spectra were fitted by a model centred with Gaussian peaks at 1628, 1680 (β-sheets), 1648, and 1661 (random coils, α-helices, and others) cm−1 123031.


Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients.

Araki K, Yagi N, Ikemoto Y, Yagi H, Choong CJ, Hayakawa H, Beck G, Sumi H, Fujimura H, Moriwaki T, Nagai Y, Goto Y, Mochizuki H - Sci Rep (2015)

The solid black line in each panel shows an FTIRM spectrum (amide I region) obtained from (A) fibrils of α-syn expressed in E. coli, (B) normal brain tissue from the patient with AD, (C) the core of an SP, (D) normal brain tissue from the brain of the patient with PD, (E) the core of an LB, and (F) the halo of an LB.Blue and red lines represent contributions of β-sheet structures and non-β-sheet structures (random coils, α-helices, and others), respectively. The dotted line represents the fitted curve. Data were fitted using a Gaussian species model centred at 1628, 1680 (β-sheets, blue line), 1648, and 1661 (random coils, α-helices, and others, red line) cm−1 123031.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4664933&req=5

f3: The solid black line in each panel shows an FTIRM spectrum (amide I region) obtained from (A) fibrils of α-syn expressed in E. coli, (B) normal brain tissue from the patient with AD, (C) the core of an SP, (D) normal brain tissue from the brain of the patient with PD, (E) the core of an LB, and (F) the halo of an LB.Blue and red lines represent contributions of β-sheet structures and non-β-sheet structures (random coils, α-helices, and others), respectively. The dotted line represents the fitted curve. Data were fitted using a Gaussian species model centred at 1628, 1680 (β-sheets, blue line), 1648, and 1661 (random coils, α-helices, and others, red line) cm−1 123031.
Mentions: Figure 3 shows the FTIR spectra of recombinant α-syn fibrils (A), of brain sections from an SP of an Alzheimer’s disease (AD) patient (Fig. 3B,C), and of an LB of an 83-year-old female PD patient (Fig. 3D–F). The spectra were fitted by a model centred with Gaussian peaks at 1628, 1680 (β-sheets), 1648, and 1661 (random coils, α-helices, and others) cm−1 123031.

Bottom Line: Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients.Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs.Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

ABSTRACT
Lewy bodies (LBs), which mainly consist of α-synuclein (α-syn), are neuropathological hallmarks of patients with Parkinson's disease (PD). The fine structure of LBs is unknown, and LBs cannot be made artificially. Nevertheless, many studies have described fibrillisation using recombinant α-syn purified from E. coli. An extremely fundamental problem is whether the structure of LBs is the same as that of recombinant amyloid fibrils. Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients. Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs. Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.

No MeSH data available.


Related in: MedlinePlus