title: Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers.
abstract: The prion protein (PrP) peptide 106-126 forms amyloid aggregates in vitro and this sequence is speculated to be involved in the formation of amyloid fibrils by the abnormally folded PrP protein (PrPSc) found in spongiform encephalopathies. It is shown here by incubation experiments in water using Thioflavin T (ThT) as a fluorescent probe for amyloid formation that changes in C-terminal charge, oxidation state and conformational stabilisation lead to large changes in amyloid forming behaviour (amyloidogenicity) of this peptide. Amyloid formation is favoured by a charged C-terminus and is strongly inhibited by oxidation. Furthermore, cationic dendrimers are shown to perturb peptide fibrillation in a process dependent on the nature of the charged groups on the dendrimer surface.
authors.affiliation: Department of Veterinary Diagnostics and Research, Danish Institute for Food and Veterinary Research, 27, Bülowsvej, DK 1790 Copenhagen V, Denmark. pmhh@dfvf.dk
authors.forename: Peter M H
authors.initials: PM
authors.lastname: Heegaard
authors.forename: Heidi Gertz
authors.initials: HG
authors.lastname: Pedersen
authors.forename: James
authors.initials: J
authors.lastname: Flink
authors.forename: Ulrik
authors.initials: U
authors.lastname: Boas
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000378:metabolism*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011328:Prions / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins
chemical_list: D000682:Amyloid; D011328:Prions; D011994:Recombinant Proteins; C466227:miniprion protein PrP106, mouse