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Local frustration determines molecular and macroscopic helix structures.

Christopher J Forman1, Szilard N Fejer, Dwaipayan Chakrabarti

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. chrisforman@cantab.net

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Decorative domains alter amyloid fiber morphology, forming spiral ribbons instead of twisted ones. This frustration principle is system-independent, impacting amyloid structure formation.

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Area of Science:

  • Biophysics
  • Materials Science
  • Molecular Biology

Background:

  • Amyloid fibers commonly form twisted ribbons, but decorative domains induce spiral ribbon morphologies.
  • Existing models often link amyloid morphology to fundamental building block interactions.

Purpose of the Study:

  • To model the effect of decorative domains on amyloid fiber morphology.
  • To investigate the role of frustration in determining amyloid structure.
  • To explore how supplementary protein sequences influence amyloid formation.

Main Methods:

  • Developed a minimal energy model of rigid building blocks (anisotropic interacting ellipsoids).
  • Perturbed the relative orientation of β strands in a bilayered extended β-sheet.
  • Used magnets to demonstrate the scale and system independence of the frustration principle.

Main Results:

  • The model predicts that the relative orientation of building blocks dictates assembly morphology.
  • Experimental amyloid structures align with the model's predictions.
  • The frustration principle was isolated from fundamental interactions, revealing its primary role in morphology determination.

Conclusions:

  • Amyloid formation can be viewed as a molecular manifestation of macroscopic frustrated bilayers.
  • Supplementary sequences like chaperones or decorative domains are crucial for stabilizing bilayers and selecting morphology.
  • The model provides a basis for studying frustration in higher-order superstructural assemblies.