FEBS Letters | |
Amyloid fibrils from the mammalian protein prothymosin α | |
Cherny, Dmitry I.1  Jovin, Thomas M.1  Subramaniam, Vinod1  Heim, Gudrun1  Pavlov, Nikolai A.1  | |
[1]Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany | |
关键词: Natively unfolded; Protein aggregation; Amyloid fibrils; Scanning force microscopy; Electron microscopy; | |
DOI : 10.1016/S0014-5793(02)02572-3 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
Mammalian prothymosin α, a small (12 kDa) and extremely acidic protein (pI 3.5), is a member of the growing family of ‘natively’ unfolded proteins. We demonstrate that at low pH (∼3) and high concentrations, prothymosin α is capable of forming regular elongated fibrils with flat ribbon structure 4–5 nm in height and 12–13 nm in width as judged from scanning force and electron microscopy. These aggregates induced a characteristic spectral shift of thioflavin T fluorescence and their circular dichroism spectra were indicative of significant β-sheet content, suggesting formation of classical amyloid. Our findings indicate that natively unfolded proteins may have a general propensity to form amyloid fibrils under conditions inducing partially folded conformations.
【 授权许可】
Unknown
【 预 览 】
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