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Related Experiment Videos

Alternative prion structural changes revealed by high pressure.

Joan Torrent1, Maria Teresa Alvarez-Martinez, Frédéric Heitz

  • 1INSERM U128, 1919 Route de Mende, F-34293 Montpellier cedex 5, France.

Biochemistry
|February 5, 2003
PubMed
Summary
This summary is machine-generated.

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High pressure can reverse heat-induced aggregation in hamster prion protein (SHaPrP), restoring its original structure. This technique allows studying prion protein refolding without aggregation artifacts.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Misfolding Diseases

Background:

  • Prion protein (PrP) misfolding and aggregation are implicated in neurodegenerative diseases.
  • Heat-induced aggregation of recombinant hamster prion protein (SHaPrP(90-231)) alters its structure from alpha-helical to beta-sheet rich.

Purpose of the Study:

  • To investigate the effect of high pressure on heat-induced prion protein aggregation.
  • To study prion protein refolding and unfolding mechanisms under pressure.
  • To characterize pressure-induced structural changes in prion protein.

Main Methods:

  • Recombinant hamster prion protein (SHaPrP(90-231)) was subjected to high temperature and then high pressure (200 MPa).
  • Structural changes were monitored using UV spectroscopy and fluorescence with 8-anilino-1-naphthalene sulfonate.

Related Experiment Videos

  • Thioflavin-T binding was used to detect further structural changes at pressures over 400 MPa.

    • Main Results:

    • High pressure (200 MPa) reversed heat-induced aggregation of SHaPrP, restoring native alpha-helical structure and tertiary structure upon pressure release.
    • Pressure-induced unfolding transitions were reversible and followed a two-state model.
    • Heat- and pressure-induced conformers exhibited different unfolding free energies.
    • Pressures exceeding 400 MPa induced a structural change leading to metastable oligomers, indicated by Thioflavin-T binding.

    Conclusions:

    • High pressure is an effective tool to prevent and reverse prion protein aggregation, enabling the study of equilibrium refolding.
    • Prion protein exhibits distinct unfolding pathways under heat and pressure.
    • Metastable oligomeric structures can form at very high pressures, suggesting complex pressure-dependent conformational landscapes.