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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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,...
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Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
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Rapid Generation of Amyloid from Native Proteins In vitro
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A versatile platform for adding functional properties to amyloid fibrils.

Devon F A Fontaine1, Valerie A Ivancic, Michael B Reardon

  • 1Carlson School of Chemistry & Biochemistry, Clark University, Worcester, MA 01610, USA. cjakobsche@clarku.edu.

Organic & Biomolecular Chemistry
|September 21, 2017
PubMed
Summary

Researchers developed novel amyloid-binding molecular tools to functionalize amyloid fibrils. These tools offer potential applications in disease research, nanomaterials development, and structural studies of fibrils.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Nanotechnology

Background:

  • Amyloid fibrils are protein aggregates implicated in various diseases.
  • Current methods for manipulating amyloid fibrils are limited.
  • Functionalizing amyloid fibrils could unlock new therapeutic and material applications.

Purpose of the Study:

  • To design and synthesize novel molecular tools capable of binding to and manipulating amyloid fibrils.
  • To impart new functional properties to amyloid fibrils using these tools.
  • To explore potential applications of these functionalized fibrils.

Main Methods:

  • Design and synthesis of a new class of amyloid-binding molecular tools.
  • Testing of prototype molecular tools for their ability to interact with amyloid fibrils.
  • Characterization of the functional properties imparted to the fibrils.

Main Results:

  • Successful design and synthesis of prototype amyloid-binding molecular tools.
  • Demonstration of the tools' ability to bind and modify amyloid fibrils.
  • Attribution of new functional properties to the manipulated amyloid fibrils.

Conclusions:

  • A new family of amyloid-binding molecular tools has been developed.
  • These tools can successfully manipulate amyloid fibrils, imparting novel functionalities.
  • Potential applications span disease-relevant fibril modification, nanomaterial development, and fibril structural studies.