Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an [alpha]-Helical Metastable Conformation

A peptide encompassing the conserved hydrophobic region and the first [beta]-strand of the prion protein (PrP(110-136)) shown to interact with the surface of dodecylphosphocholine micelles adopts an [alpha]-helical conformation that is localized below the head-group layer. This surface-bound peptide...

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Bibliographic Details
Published in:PloS one 2016-12, Vol.11 (12), p.e0168021
Main Authors: Sauvé, Simon, Aubin, Yves
Format: Article
Language:English
Subjects:
Amyloid beta-protein
Analysis
Nuclear magnetic resonance spectroscopy
Prions (Proteins)
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Summary:A peptide encompassing the conserved hydrophobic region and the first [beta]-strand of the prion protein (PrP(110-136)) shown to interact with the surface of dodecylphosphocholine micelles adopts an [alpha]-helical conformation that is localized below the head-group layer. This surface-bound peptide has a half-life of one day, and readily initiates the formation of amyloid fibrils. The presence of the latter was confirmed using birefringence microscopy upon Congo red binding and thioflavin T-binding induced fluorescence. The observation of this metastable [alpha]-helical conformer provides a unique snapshot of the early steps of the inter-conversion pathway. These findings together with the body of evidence from the prion literature allowed us to propose a mechanism for the conversion of PrP.sup.C to amyloid material.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0168021