Amyloid fibrils from the mammalian protein prothymosin α

FEBS Letters

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.

【 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