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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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Related Experiment Video

Updated: May 28, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Probing small molecule binding to amyloid fibrils.

Alexander K Buell1, Elin K Esbjörner, Patrick J Riss

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

Physical Chemistry Chemical Physics : PCCP
|October 19, 2011
PubMed
Summary

Researchers explored biophysical methods to study small molecule interactions with amyloid fibrils. New techniques like linear dichroism and biosensing offer direct insights into these crucial molecular binding events for disease research.

Related Experiment Videos

Last Updated: May 28, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Area of Science:

  • Biophysics
  • Molecular Biology
  • Biochemistry

Background:

  • Amyloid fibrils and protein aggregates are implicated in various diseases.
  • Understanding small molecule interactions with these aggregates is crucial for developing diagnostics and therapeutics.

Purpose of the Study:

  • To provide an overview of biophysical methods for studying amyloid-small molecule interactions.
  • To highlight the utility of linear dichroism and biosensing techniques in this field.

Main Methods:

  • Review of established and emerging biophysical techniques.
  • Detailed discussion of linear dichroism (LD) spectroscopy.
  • Explanation of biosensing approaches for amyloid-small molecule binding detection.

Main Results:

  • Linear dichroism offers a sensitive extension to traditional spectroscopic methods.
  • Biosensing methods provide direct measurement of small molecule binding to surface-immobilized amyloid fibrils.
  • Both discussed techniques offer direct links to the physical properties associated with binding events.

Conclusions:

  • Linear dichroism and biosensing are valuable tools for investigating amyloid-small molecule interactions.
  • These methods facilitate a deeper understanding of molecular mechanisms in protein aggregation diseases.
  • Advancements in biophysical techniques are key to developing targeted diagnostic and therapeutic strategies.