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Updated: Sep 13, 2025

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Structural and thermodynamic classification of amyloid polymorphs.

Jack P Connor1, Sheena E Radford1, David J Brockwell1

  • 1Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.

Structure (London, England : 1993)
|July 29, 2025
PubMed
Summary
This summary is machine-generated.

Amyloid fibril structures, though diverse, can be classified into distinct families based on their topology. This framework aids in comparing disease-related and in vitro amyloids.

Keywords:
amyloidhierarchical clusterpolymorphismtauthermodynamicsα-synuclein

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Over 500 amyloid structures are known, revealing diverse fibril architectures.
  • These structures generally conform to the cross-β amyloid fold.

Purpose of the Study:

  • To develop a hierarchical classification system for amyloid fibril structures.
  • To enable systematic comparison of amyloid structures from different sources.

Main Methods:

  • Hierarchical clustering of amyloid structures (e.g., alpha-synuclein, tau).
  • Energy profiling using FoldX to identify stabilizing regions.
  • Comparative analysis of fibril topologies and stability.

Main Results:

  • Amyloid fibrils can be grouped into distinct topological fold families.
  • Despite varied topologies, fibrils share similar energy profiles and stabilizing regions.
  • Specific regions stabilize the amyloid core through different pairing interactions.

Conclusions:

  • A framework is established for classifying new amyloid structures based on topology.
  • This classification facilitates comparisons between in vivo and in vitro amyloid fibrils.
  • An automated workflow allows for rapid analysis of emerging amyloid structures.