Amyloid fibrils from the mammalian protein prothymosin alpha.
FEBS Lett
; 517(1-3): 37-40, 2002 Apr 24.
Article
em En
| MEDLINE
| ID: mdl-12062405
ABSTRACT
Mammalian prothymosin alpha, 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 ( approximately 3) and high concentrations, prothymosin alpha 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 beta-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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Precursores de Proteínas
/
Tiazóis
/
Timosina
/
Peptídeos beta-Amiloides
Limite:
Humans
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2002
Tipo de documento:
Article
País de afiliação:
Alemanha