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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...
Total Internal Reflection Fluorescence Microscopy01:05

Total Internal Reflection Fluorescence Microscopy

Total internal reflection fluorescence microscopy or TIRF is an advanced microscopic technique used to visualize fluorophores in samples close to a solid surface with a higher refractive index, such as a glass coverslip. TIRF only allows fluorophores in proximity to the solid surface to be excited. When light from a medium with a lower refractive index (such as air) hits the glass coverslip at a critical angle, the light undergoes total internal reflection stead of passing through the glass.

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Related Experiment Video

Updated: May 27, 2026

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

Nanomaterials: amyloids reflect their brighter side.

Shruti Mankar1, A Anoop, Shamik Sen

  • 1Department of Biosciences and Bioengineering, Indian Institute of Technology, Bombay.

Nano Reviews
|November 24, 2011
PubMed
Summary

Amyloid fibrils, self-assembled protein nanostructures, show potential in nanomaterials. Functional amyloids, distinct from disease-related forms, offer novel applications in nanotechnology and biomedicine.

Keywords:
Nanotechnologydrug deliveryfibrilsnanowirespeptide/proteinself-assemblystem cellstissue engineering

More Related Videos

Polarization-Sensitive Two-Photon Microscopy for a Label-Free Amyloid Structural Characterization
05:54

Polarization-Sensitive Two-Photon Microscopy for a Label-Free Amyloid Structural Characterization

Published on: September 8, 2023

Related Experiment Videos

Last Updated: May 27, 2026

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

Polarization-Sensitive Two-Photon Microscopy for a Label-Free Amyloid Structural Characterization
05:54

Polarization-Sensitive Two-Photon Microscopy for a Label-Free Amyloid Structural Characterization

Published on: September 8, 2023

Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Molecular Biology

Background:

  • Amyloid fibrils are ordered nanostructures formed from proteins.
  • These rigid, mechanically strong structures are linked to human diseases.
  • However, some amyloids, termed functional amyloids, have native biological roles.

Purpose of the Study:

  • To review recent advancements in utilizing amyloid fibrils for nanomaterial development.
  • To explore prospective applications of amyloid-based nanomaterials in nanotechnology and biomedicine.

Main Methods:

  • Literature review of scientific publications on amyloid fibrils and nanomaterials.
  • Analysis of studies focusing on functional amyloids and their material properties.
  • Synthesis of information on applications in nanotechnology and biomedicine.

Main Results:

  • Amyloid fibrils offer a versatile platform for creating novel nanomaterials.
  • Functional amyloids present unique opportunities for bio-inspired material design.
  • Emerging applications span diagnostics, therapeutics, and advanced material engineering.

Conclusions:

  • Amyloid fibrils are promising building blocks for advanced nanomaterials.
  • Functional amyloids represent a key area for innovation in biomaterials.
  • Further research into amyloid-based materials will drive progress in nanotechnology and medicine.