Morphology and secondary structure of stable beta-oligomers formed by amyloid peptide PrP(106-126).
Biochemistry
; 48(25): 5779-81, 2009 Jun 30.
Article
em En
| MEDLINE
| ID: mdl-19476383
ABSTRACT
The formation of nonfibrillar oligomers has been proposed to be a common element of the aggregation pathway of amyloid peptides. Here we describe the first detailed investigation of the morphology and secondary structure of stable oligomers formed by a peptide comprising residues 106-126 of the human prion protein (PrP). These oligomers have an apparent hydrodynamic radius of approximately 30 nm and are more membrane-active than monomeric or fibrillar PrP(106-126). Circular dichroism and solid state NMR data support formation of an extended beta-strand by the hydrophobic core of PrP(106-126), while negative thioflavin-T binding implies an absence of cross-beta structure in nonfibrillar oligomers.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Príons
/
Amiloide
Limite:
Humans
Idioma:
En
Ano de publicação:
2009
Tipo de documento:
Article