title: Observation of sequence specificity in the seeding of protein amyloid fibrils.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
authors.forename: Mark R H
authors.initials: MR
authors.lastname: Krebs
authors.forename: Ludmilla A
authors.initials: LA
authors.lastname: Morozova-Roche
authors.forename: Katie
authors.initials: K
authors.lastname: Daniel
authors.forename: Carol V
authors.initials: CV
authors.lastname: Robinson
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Dobson
mesh_terms: 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
chemical_list: D046912:Multiprotein Complexes; D009113:Muramidase