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Related Concept Videos

Amyloid Fibrils03:03

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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. 
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The Proteasome02:18

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
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Updated: Sep 23, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
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A proteolytic functional amyloid digests pathogenic amyloids.

Tanmay Mondal1, Bhubaneswar Mandal1

  • 1Department of Chemistry, Indian Institute of Technology Guwahati, Assam 781039, India. bmandal@iitg.ac.in.

Journal of Materials Chemistry. B
|May 17, 2022
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Summary

Researchers engineered functional amyloids to destroy pathogenic amyloids. These novel amyloid destructors selectively degrade amyloid-beta proteins, offering a new therapeutic strategy for amyloid diseases.

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Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers
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Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers
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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Drug Discovery

Background:

  • Pathogenic amyloids are implicated in numerous diseases, with limited therapeutic options.
  • Functional amyloids, beneficial protein aggregates, can be engineered for specific tasks.
  • Current drug development for amyloidosis has a high failure rate, necessitating novel approaches.

Purpose of the Study:

  • To design and characterize novel amyloid-destroying functional amyloids (PFAs).
  • To investigate the mechanism and efficacy of PFAs in degrading pathogenic amyloids.
  • To establish a new platform for targeted protein degradation.

Main Methods:

  • Rational design of a catalytic triad-based proteolytic functional amyloid (PFA).
  • Integration of a target protein recognition unit with a Gly-integrated Glu-His-Cys segment.
  • MALDI-TOF and FRET-based analyses for cleavage and degradation studies.

Main Results:

  • Designed PFAs demonstrated selective cleavage of Aβ12-21 and pathogenic Aβ1-40 in vitro.
  • PFAs effectively inhibited Aβ1-40 aggregation.
  • Preformed amyloid fibrils were broken down into non-toxic metabolites by PFAs.

Conclusions:

  • PFAs represent the first class of "amyloid-destroying" amyloids.
  • This platform offers a novel strategy for the chemical degradation of pathogenic amyloids.
  • The PFA technology may be applicable for targeted degradation of other harmful proteins.