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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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Updated: Oct 31, 2025

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
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Functionalized Prion-Inspired Amyloids for Biosensor Applications.

Marta Díaz-Caballero1, Susanna Navarro1, Salvador Ventura1

  • 1Institut de Biotecnologia i de Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Bellaterra (Barcelona), Spain.

Biomacromolecules
|July 1, 2021
PubMed
Summary
This summary is machine-generated.

Researchers developed a new method to create functional protein amyloid nanofibers using the biotin-streptavidin system. This approach allows for versatile modification of nanomaterials for diverse applications.

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Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Protein Engineering

Background:

  • Protein amyloid nanofibers offer biocompatible platforms for nanomaterials but have limited functionality.
  • Current methods for modifying amyloid nanostructures are complex and costly.

Purpose of the Study:

  • To develop a simple, modular, and versatile strategy for functionalizing amyloid-based nanomaterials.
  • To exploit the biotin-streptavidin system for on-demand tailoring of amyloid nanostructures.

Main Methods:

  • Prion-inspired heptapeptides were doped with biotin-conjugated counterparts.
  • Biotinylated peptides were assembled into amyloid-like fibers under mild conditions.
  • Fibers were functionalized with various streptavidin conjugates (gold nanoparticles, quantum dots, enzymes).

Main Results:

  • Demonstrated versatile functionalization of amyloid scaffolds with streptavidin conjugates.
  • Achieved specific functionalization with peroxidase and phosphatase activities.
  • Created a nanostructured glucose biosensor by simultaneous functionalization with two enzymes.

Conclusions:

  • Presented a simple, modular, and multivalent approach for developing functional amyloid nanomaterials.
  • Enabled facile decoration of amyloid fibers with diverse chemical and biological moieties.
  • Opened new avenues for creating advanced amyloid-based nanostructures for various applications.