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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Published on: September 12, 2019

Amyloids: not only pathological agents but also ordered nanomaterials.

Izhack Cherny1, Ehud Gazit

  • 1The Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel.

Angewandte Chemie (International Ed. in English)
|April 17, 2008
PubMed
Summary

Amyloid fibers are abundant natural assemblies formed by proteins and peptides. These stable structures offer unique properties and diverse applications, surpassing synthetic polymers.

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Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Materials Science

Background:

  • Amyloid fibers are prevalent, naturally occurring self-assembled structures.
  • These fibers are formed by diverse protein and peptide molecules under various conditions.
  • They exhibit stability and organized structures, including liquid crystals and nanotubes.

Purpose of the Study:

  • To review the structural characteristics of amyloidal supramolecular assemblies.
  • To discuss the potential use of natural and de novo designed sequences.
  • To highlight demonstrated applications of these assemblies.

Main Methods:

  • Literature review of structural characteristics.
  • Analysis of natural and de novo designed sequences.
  • Compilation of demonstrated applications.

Main Results:

  • Amyloid fibers exhibit diverse structural properties and phase states.
  • Both natural and designed sequences can form these assemblies.
  • Applications span various fields due to combined biological and mechanical properties.

Conclusions:

  • Amyloidal supramolecular assemblies possess unique structural and functional attributes.
  • Their potential applications are extensive and exceed those of synthetic polymers.
  • Further research into de novo design can unlock novel uses.