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The expanding amyloid family: Structure, stability, function, and pathogenesis.

Michael R Sawaya1, Michael P Hughes1, Jose A Rodriguez1

  • 1Departments of Chemistry and Biochemistry and Biological Chemistry, UCLA, Los Angeles, CA 90095, USA; Howard Hughes Medical Institute, UCLA, Los Angeles, CA 90095, USA; UCLA-DOE Institute, UCLA, Los Angeles, CA 90095, USA; Molecular Biology Institute, UCLA, Los Angeles, CA 90095, USA.

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Amyloid proteins form fibrils with diverse structures, influencing disease and function. Structural frustration explains their conformational variability and adaptability.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Amyloid proteins are known for their role in diseases like Alzheimer's.
  • These proteins adopt unique fibrillar structures distinct from globular proteins.
  • A single protein sequence can form different amyloid structures (polymorphs).

Purpose of the Study:

  • To explore the atomic-level structures of various amyloid fibrils.
  • To understand the conformational variability and structural basis of amyloid function and pathogenicity.
  • To investigate the role of structural frustration in amyloid behavior.

Main Methods:

  • High-resolution structural analysis of over 80 amyloid fibrils.
  • Comparative analysis of pathogenic and functional amyloid structures.
  • Investigation into the relationship between protein sequence, conformation, and fibril properties.

Main Results:

  • Detailed atomic structures of numerous amyloid protein fibrils have been elucidated.
  • Identified over 80 distinct amyloid fibril structures, including pathogenic and functional types.
  • Demonstrated that conformational variability, driven by structural frustrations, is key to amyloid function and disease.

Conclusions:

  • Amyloid structure is highly plastic, with a single sequence capable of forming diverse fibril polymorphs.
  • Structural frustration is a critical determinant of amyloid fibril stability, sensitivity, and biological function.
  • Understanding amyloid conformational diversity is essential for deciphering their roles in health and disease.