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Physical and structural basis for polymorphism in amyloid fibrils.

Robert Tycko1

  • 1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, 20892-0520.

Protein Science : a Publication of the Protein Society
|September 3, 2014
PubMed
Summary

Amyloid fibrils have defined structures, but these are not solely dictated by their amino acid sequences. Molecular polymorphism in amyloid structures is common and influenced by physical factors.

Keywords:
Alzheimer's diseaseamyloid structurefibril structureprionsolid state NMR

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Amyloid fibrils are protein aggregates implicated in various diseases.
  • Understanding their molecular structure is crucial for disease mechanism insights.

Purpose of the Study:

  • To review current knowledge on amyloid fibril structures.
  • To discuss the phenomenon of amyloid polymorphism and its underlying causes.
  • To explore the biological significance of amyloid polymorphism.

Main Methods:

  • Review of existing literature on amyloid fibril structures.
  • Focus on solid-state nuclear magnetic resonance (ssNMR) data.
  • Analysis of physical principles governing polymorphism.

Main Results:

  • Amyloid fibril structures are well-defined but not uniquely determined by sequence.
  • Self-propagating molecular polymorphism is a common characteristic.
  • Physical factors play a key role in the development and persistence of polymorphism.

Conclusions:

  • Amyloid polymorphism is a widespread phenomenon.
  • Understanding polymorphism is essential for comprehending amyloid diseases.
  • Principles discussed apply broadly to various amyloid-forming peptides and proteins.