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Amyloid aggregates of the prion peptide PrP106–126 are destabilised by oxidation and by the action of dendrimers
Author(s) -
Heegaard Peter M.H.,
Pedersen Heidi Gertz,
Flink James,
Boas Ulrik
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.09.073
Subject(s) - thioflavin , peptide , amyloid (mycology) , chemistry , dendrimer , biophysics , in vitro , fibril , cationic polymerization , biochemistry , intracellular , fluorescence , polymer chemistry , biology , alzheimer's disease , medicine , pathology , inorganic chemistry , physics , disease , quantum mechanics
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 (PrP Sc ) 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.