Conformational plasticity of the Gerstmann-Sträussler-Scheinker disease peptide as indicated by its multiple aggregation pathways.

  title={Conformational plasticity of the Gerstmann-Str{\"a}ussler-Scheinker disease peptide as indicated by its multiple aggregation pathways.},
  author={Antonino Natalello and Valery V Prokorov and F. Tagliavini and Michela Morbin and Gianluigi Forloni and Marten Beeg and Claudia Manzoni and Laura Colombo and Marco Gobbi and Mario Salmona and Silvia Maria Doglia},
  journal={Journal of molecular biology},
  volume={381 5},
The existence of several prion strains and their capacity of overcoming species barriers seem to point to a high conformational adaptability of the prion protein. To investigate this structural plasticity, we studied here the aggregation pathways of the human prion peptide PrP82-146, a major component of the Gerstmann-Sträussler-Scheinker amyloid disease. By Fourier transform infrared (FT-IR) spectroscopy, electron microscopy, and atomic force microscopy (AFM), we monitored the time course of… CONTINUE READING