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J. Biol. Chem., Vol. 269, Issue 11, 7859-7862, 03, 1994
L De Gioia, C Selvaggini, E Ghibaudi, L Diomede, O Bugiani, G Forloni, F Tagliavini and M Salmona
Prion-related encephalopathies are characterized by cerebral accumulation
of a post-translationally modified form of the cellular prion protein
(PrPC), designated PrPSc. Evidence suggests that the conversion from PrPC
to PrPSc involves changes in the secondary structure leading to an increase
in beta-sheet content. We have previously shown that a synthetic peptide
homologous to residues 106- 126 of human PrP, belonging to a predicted
alpha-helical domain, exhibits a beta-sheet conformation, forms
amyloid-like fibrils, and is neurotoxic in vitro. The present study
investigated how different chemicophysical conditions such as pH and ionic
strength or a membrane- like environment influenced the secondary structure
of this peptide. PrP 106-126 exhibited a predominantly beta-sheet structure
in 200 mM phosphate buffer, pH 5.0, but a combination of beta-sheet and
random coil structure in 200 mM phosphate buffer, pH 7.0, or in deionized
water. The addition of trifluoroethanol (50% final concentration) to
solutions of peptide in deionized water induced the appearance of an
alpha-helical secondary structure, but did not modify the beta-sheet
conformation of the peptide dissolved in 200 mM phosphate buffer, pH 5.0.
In the presence of micelles formed by a 5% solution of sodium dodecyl
sulfate, PrP 106-126 showed a high content of alpha-helix. When the peptide
was dissolved in 5 mM phosphate buffer, pH 7.4, and incubated with
liposomes, it changed from a prevalently randon coil structure to a
beta-sheet conformation. The environment-dependent conformational
polymorphism of PrP 106-126 and its marked tendency to form stable
beta-sheet structures at acidic pH could account for the shift from
alpha-helix to beta-sheet associated with the conversion of PrPC to PrPSc,
which occurs most likely in the endosomal-lysosomal compartment.
Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein
Istituto di Richerche Farmacologiche Mario Negri, Milan, Italy.
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