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Probing the early stages of prion protein (PrP) aggregation with atomistic molecular dynamics simulations

Francesca Collu1, Enrico Spiga, Nesrine Chakroun

  • 1King's College London, Randall Centre for Cell & Molecular Biophysics, London, UK. franca.fraternali@kcl.ac.uk.

Chemical Communications (Cambridge, England)
|July 4, 2018
PubMed

Insights

Prion diseases involve misfolded proteins called prions. This study used molecular dynamics simulations to investigate the aggregation of the ovine prion protein

Area of Science:

  • Protein Misfolding Diseases
  • Structural Biology
  • Computational Biophysics

Background:

  • Prions are infectious agents composed of misfolded proteins.
  • Prion protein (PrP) misfolding leads to amyloid fibril formation.
  • The H2H3 domain of ovine prion protein (H2H3-OvPrPSc) is implicated in oligomerization.

Purpose of the Study:

  • To investigate the aggregation process of the H2H3-OvPrPSc domain.
  • To understand the molecular mechanisms of prion oligomerization.
  • To utilize molecular dynamics simulations for prion research.

Main Methods:

  • Molecular dynamics (MD) simulations.
  • Analysis of protein aggregation pathways.
  • Structural characterization of amyloid-like fibrils.

Main Results:

  • Simulations revealed key steps in the aggregation of H2H3-OvPrPSc.
  • Identified conformational changes leading to amyloid-like fibril formation.
  • Provided insights into the role of the β-rich H2H3 domain in prion aggregation.

Conclusions:

  • The H2H3 domain plays a critical role in prion protein aggregation.
  • Molecular dynamics simulations are valuable for studying prion conformational changes.
  • Understanding these mechanisms can inform strategies against prion diseases.

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