2016 Fiscal Year Annual Research Report
Study on cold and heat denaturation of amyloid fibrils of intrinsically disordered alpha-synuclein
| Project/Area Number |
15K18518
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| Research Institution | Osaka University |
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Principal Investigator |
李 映昊 大阪大学, たんぱく質研究所, 講師 (70589431)
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Keywords | Alpha-synuclein / Amyloid fibril / Cold denaturation / Heat denaturation / Kinetics / Protein aggregation / Protein misfolding / Thermodynamics |
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| Outline of Annual Research Achievements |
Although the structural stability of globular proteins has been extensively examined, the conformational stability of disease-induced amyloid fibrils is largely unknown. Thus, I performed in-depth studies on the conformational stability of amyloid fibrils at a wide range of temperature. I examined cold and heat denaturation of amyloid fibrils of intrinsically disordered alpha-synuclein (aSN) prepared at various temperatures (298, 310, 323, 333, and 343 K). Formation of typical amyloid fibrils was confirmed by ThT assay, far-UV CD spectra, and AFM images at all temperatures. Despite differences in temperature for aSN amyloidogenesis, all fibrils showed similar core regions with distinct fibril height (i.e., width). As temperature increased from 298 to 383 K, all types of aSN fibrils heat-denatured to monomers from approximately 343 K. Decreasing temperature from 298 to 273 K caused cold denaturation of fibrils to monomers. Intriguingly, the stability of aSN fibrils depended on temperature of preparation of aSN fibrils. aSN fibrils generated at higher temperature showed higher stability at high and low temperature than fibrils formed at lower temperature. aSN fibrils prepared at higher temperature were more resistant against chemical stress than fibrils formed at lower temperature. As temperature where aSN fibrils grow increased, fibrils also showed slower cold, heat, and chemical denaturation. Taken together, the stability of aSN amyloid fibrils depended on growing temperature of fibrils which produced differences in higher order structures of amyloid fibrils.
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Research Products
(20 results)
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[Journal Article] A. Reduced Lipid Bilayer Thickness Regulates the Aggregation and Cytotoxicity of Amyloid-β2017
Author(s)
Kyle J. Korshavn, Cristina Satriano, Yuxi Lin, Rongchun Zhang, Mark Dulchavsky, Anirban Bhunia, Magdalena I. Ivanova, Young-Ho Lee, Carmelo La Rosa, Mi Hee Lim, Ayyalusamy Ramamoorthy
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Journal Title
J. Biol. Chem.
Volume: 292
Pages: 4638-4650
DOI
Peer Reviewed / Int'l Joint Research
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[Journal Article] Energetic basis on interactions between ferredoxin and ferredoxin NADP+ reductase at varying physiological conditions2017
Author(s)
Misaki Kinoshita, Ju Yaen Kim, Satoshi Kume, Yuxi Lin, K. Hun Mok, Yosky Kataoka, Koichiro Ishimori, Natalia Markova, Genji Kurisu, Toshiharu Hase, Young-Ho Lee
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Journal Title
Biochem. Biophys. Res. Commun.
Volume: 482
Pages: 909-915
DOI
Peer Reviewed / Int'l Joint Research
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[Journal Article] Noncovalent Forces Tune the Electron Transfer Complex between Ferredoxin and Sulfite Reductase to Optimize Enzymatic Activity2016
Author(s)
Ju Yaen Kim, Misaki Kinoshita, Satoshi Kume, Guy T. Hanke, Toshihiko Sugiki, John E. Ladbury, Chojiro Kojima, Takahisa Ikegami, Genji Kurisu, Yuji Goto, Toshiharu Hase, Young-Ho Lee
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Journal Title
Biochem J.
Volume: 473
Pages: 3837-3854
DOI
Peer Reviewed / Int'l Joint Research
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[Journal Article] Mutations Affecting the Internal Equilibrium of the 6-aminohexano-atedimer Hydrolase Reaction2016
Author(s)
Seiji Negoro, Yasuyuki Kawashima1, Naoki Shibata, Tatsuya Kobayashi, Takeshi Baba, Young-Ho Lee, Katsumasa Kamiya, Yasuteru Shigeta, Keisuke Nagai, Ikki Takehara, Dai-ichiro Kato, Masahiro Takeo, Yoshiki Higuchi
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Journal Title
FEBS Lett.
Volume: 590
Pages: 3133-3143
DOI
Peer Reviewed
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