NR ANAU
AU Zou,W.Q.; Yang,D.S.; Fraser,P.E.; Cashman,N.R.; Chakrabartty,A.
TI All or none fibrillogenesis of a prion peptide
QU European Journal of Biochemistry 2001 Sep; 268(18): 4885-91
PT journal article
AB Amyloid proteins and peptides comprise a diverse group of molecules that vary both in size and amino-acid sequence, yet assemble into amyloid fibrils that have a common core structure. Kinetic studies of amyloid fibrillogenesis have revealed that certain amyloid proteins form oligomeric intermediates prior to fibril formation. We have investigated fibril formation with a peptide corresponding to residues 195-213 of the human prion protein. Through a combination of kinetic and equilibrium studies, we have found that the fibrillogenesis of this peptide proceeds as an all-or-none reaction where oligomeric intermediates are not stably populated. This variation in whether oligomeric intermediates are stably populated during fibril formation indicates that amyloid proteins assemble into a common fibrillar structure; however, they do so through different pathways.
MH Amino Acid Sequence; Animal; Circular Dichroism; Energy Transfer; Human; Hydrogen-Ion Concentration; Kinetics; Microscopy, Electron; Molecular Sequence Data; Naphthalenesulfonates; Nephelometry and Turbidimetry; Peptide Fragments/*chemistry/*metabolism; Prions/*chemistry/*metabolism; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Spectrometry, Fluorescence; Support, Non-U.S. Gov't
AD Wen-Quan Zou, Dun-Sheng Yang, Paul E. Fraser, Neil R. Cashman, Centre for Research in Neurodegenerative Diseases; Paul E. Fraser, Avijit Chakrabartty, Department of Medical Biophysics, University of Toronto, Ontario, Canada
SP englisch
PO Deutschland