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Related Experiment Video

Updated: Feb 11, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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Conformational evolution of polymorphic amyloid assemblies.

Chen Liang1, Ming-Chien Hsieh1, Noel X Li1

  • 1Department of Chemistry, Emory University, Atlanta, GA 30322, United States.

Current Opinion in Structural Biology
|May 6, 2018
PubMed
Summary
This summary is machine-generated.

Amyloid assemblies exhibit diverse structures, complicating therapies. This review proposes "conformational evolution," where amyloid structures change and adapt during assembly, influencing disease and biomaterial development.

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Last Updated: Feb 11, 2026

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Area of Science:

  • Biochemistry
  • Biomaterials Science
  • Structural Biology

Background:

  • Amyloid assemblies display significant morphological diversity, hindering therapeutic development and biomaterial design.
  • Understanding the dynamic nature of amyloid formation is crucial for addressing associated diseases and creating new materials.

Purpose of the Study:

  • To review the conformational evolution of amyloid assemblies from initial phase separation to ordered structures.
  • To propose the concept of conformational evolution, highlighting structural transitions and selection pressures during amyloid assembly.

Main Methods:

  • Literature review of amyloid assembly pathways.
  • Analysis of evidence for structural transitions in amyloid assemblies.
  • Conceptual framework development for conformational evolution.

Main Results:

  • Amyloid formation progresses through distinct phases: liquid-liquid phase separation, oligomeric particles, and ordered assemblies.
  • Amyloid structures emerging from oligomeric phases may be unstable and undergo further transitions.
  • Structural mutations at fiber ends or surfaces are proposed to be under selection during assembly.

Conclusions:

  • The concept of conformational evolution provides a framework for understanding amyloid morphological diversity.
  • This framework has implications for developing targeted therapies for amyloid-related diseases.
  • Understanding conformational evolution is key to designing novel amyloid-based biomaterials.