Morphology and secondary structure of stable beta-oligomers formed by amyloid peptide PrP(106-126).
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.
Walsh
Patrick
P
Molecular Structure and Function Program, Hospital for Sick Children, Toronto, ON, Canada M5G 1X8.
Yau
Jason
J
Simonetti
Karen
K
Sharpe
Simon
S
D000682:Amyloid / Q000737:chemistry* / Q000633:toxicity / Q000648:ultrastructure; D002942:Circular Dichroism; D006801:Humans; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000633:toxicity / Q000648:ultrastructure; D011328:Prions / Q000737:chemistry* / Q000633:toxicity / Q000648:ultrastructure; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D000682:Amyloid; D010446:Peptide Fragments; D011328:Prions; C082632:prion protein (106-126)