A peptide encompassing the conserved hydrophobic region and the first β-strand of the prion protein (PrP(110-136)) shown to interact with the surface of dodecylphosphocholine micelles adopts an α-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 α-helical conformer provides a unique snapshot of the early steps of the interconversion pathway. These findings together with the body of evidence from the prion literature allowed us to propose a mechanism for the conversion of PrPC to amyloid material.

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Persistent URL dx.doi.org/10.1371/journal.pone.0168021
Journal PLoS ONE
Sauvé, S. (Simon), & Aubin, Y. (2016). Dodecylphosphocholine micelles induce amyloid formation of the PrP(110-136) Peptide via an α-Helical metastable conformation. PLoS ONE, 11(12). doi:10.1371/journal.pone.0168021