Amyloid structures: much more than just a cross-β fold.

Area of Science:

• Biochemistry
• Structural Biology
• Neuroscience

Background:

• Amyloid structures are implicated in neurodegenerative diseases.
• Previous understanding of amyloid structure was limited.

Purpose of the Study:

• To discuss the diversity and complexity of amyloid structures.
• To highlight factors contributing to amyloid structural variation.

Main Methods:

• Cryo-electron microscopy
• Electron diffraction
• Solid-state Nuclear Magnetic Resonance (NMR)

Main Results:

• High-resolution structures of amyloid fibrils were obtained.
• Amyloid structures exhibit unexpected diversity beyond the cross-beta fold.
• Identified variations include dynamic regions, ligand binding motifs, cavities, non-protein components, and polymorphism.

Conclusions:

• The amyloid fold is more complex and diverse than previously understood.
• Structural variations in amyloid fibrils may influence their role in disease pathogenesis.