Observation of sequence specificity in the seeding of protein amyloid fibrils.
It is well established that the rate of formation of fibrils by amyloidogenic proteins is enhanced by the addition of preformed fibrils, a phenomenon known as seeding. We show that the efficiency of seeding fibril formation from solutions of hen lysozyme by a series of other proteins depends strongly on the similarity of their sequences. This observation is consistent with the importance of long-range interactions in stabilizing the core structure of amyloid fibrils and may be associated with the existence of a species barrier observed in the transmissible spongiform encephalopathies. In addition, it is consistent with the observation of a single dominant type of protein in the deposits associated with each form of amyloid disease.
Krebs
Mark R H
MR
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Morozova-Roche
Ludmilla A
LA
Daniel
Katie
K
Robinson
Carol V
CV
Dobson
Christopher M
CM
D000818:Animals; D002645:Chickens; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D017096:Prion Diseases / Q000378:metabolism; D017510:Protein Folding; D013045:Species Specificity; D013057:Spectrum Analysis
D046912:Multiprotein Complexes; D009113:Muramidase