Molecular origin of Gerstmann-Sträussler-Scheinker syndrome: insight from computer simulation of an amyloidogenic prion peptide.

@article{Daidone2011MolecularOO,
  title={Molecular origin of Gerstmann-Str{\"a}ussler-Scheinker syndrome: insight from computer simulation of an amyloidogenic prion peptide.},
  author={Isabella Daidone and Alfredo di Nola and Jeremy C. Smith},
  journal={Biophysical journal},
  year={2011},
  volume={100 12},
  pages={3000-7}
}
Prion proteins become pathogenic through misfolding. Here, we characterize the folding of a peptide consisting of residues 109-122 of the Syrian hamster prion protein (the H1 peptide) and of a more amyloidogenic A117V point mutant that leads in humans to an inheritable form of the Gerstmann-Sträussler-Scheinker syndrome. Atomistic molecular dynamics simulations are performed for 2.5 μs. Both peptides lose their α-helical starting conformations and assume a β-hairpin that is structurally similar… CONTINUE READING
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Publications referenced by this paper.
Showing 1-10 of 54 references

Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent

  • A. De Simone, P. Derreumaux
  • J. Chem. Phys. 132:165103
  • 2010

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