Open AccessAll or none fibrillogenesis of a prion peptide
Author(s) -
Zou WenQuan,
Yang DunSheng,
Fraser Paul E.,
Cashman Neil R.,
Chakrabartty Avijit
Publication year - 2001
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2001.02415.x
Subject(s) - fibrillogenesis , fibril , peptide , chemistry , amyloid fibril , amyloid (mycology) , biophysics , peptide sequence , biochemistry , protein structure , amyloid disease , protein folding , amyloid β , biology , medicine , inorganic chemistry , disease , pathology , gene
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.