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David Punihaole1, Ryan S Jakubek1, Riley J Workman2

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This summary is machine-generated.

Polyglutamine (polyQ) peptide Q10 exhibits distinct solution states with high interconversion barriers. Acetonitrile induces reversible fibril formation, offering new insights into polyQ structural transitions.

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Area of Science:

  • Biophysics
  • Computational Chemistry
  • Materials Science

Background:

  • Polyglutamine (polyQ) peptides are implicated in neurodegenerative diseases.
  • Understanding polyQ conformational dynamics is crucial for disease mechanism elucidation.

Purpose of the Study:

  • Investigate the solution and fibril conformations of the polyglutamine peptide D2Q10K2 (Q10).
  • Elucidate the structural transitions and activation barriers between different Q10 conformational states.
  • Explore the mechanisms of reversible polyQ fibril formation.

Main Methods:

  • Synergistic use of UV resonance Raman (UVRR) spectroscopy and molecular dynamics (MD) simulations.
  • Metadynamics simulations to explore the conformational energy landscape.
  • Electron microscopy to characterize aggregate morphology.

Main Results:

  • Q10 exists in two distinct monomeric solution states: a collapsed β-strand and a PPII-like structure with a high activation barrier.
  • Acetonitrile promotes conversion to α-helix-like structures and β-sheet aggregates.
  • PolyQ aggregates formed in acetonitrile are reversible, redissolving in water.

Conclusions:

  • Q10 peptides sample broad conformational landscapes with significant activation barriers between states.
  • Reversible polyQ fibril formation is demonstrated, challenging previous understandings.
  • Provides molecular-level insights into polyQ conformations and fibril formation pathways.