Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers

Peter M H Heegaard, Heidi Gertz Pedersen, James Flink, Ulrik Boas
FEBS Letters 2004 November 5, 577 (1): 127-33
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.

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