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Amyloid Fibrils

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,...

Amyloid Fibrils

Amyloid Fibrils

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Related Experiment Video

Updated: May 4, 2026

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease

Published on: April 19, 2021

Amyloid cannot resist identification.

Dmitry Kryndushkin¹, Maggie P Wear¹, Frank Shewmaker¹

¹Department of Pharmacology; Uniformed Services University of the Health Sciences; Bethesda, MD USA.

|December 25, 2013

Summary

This summary is machine-generated.

Many proteins can form amyloid fibrils, which are linked to diseases. This study identifies proteins that aggregate with amyloid, potentially revealing new disease mechanisms.

Keywords:

amyloid polyglutamine prion protein aggregation yeast

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Published on: October 20, 2017

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

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Published on: October 20, 2017

Area of Science:

Biochemistry
Cell Biology
Neurodegenerative Diseases

Background:

Amyloid fibril formation is a common protein polymerization process.
While some amyloids are functional, aberrant aggregation is linked to pathogenesis.
The exact role of amyloid fibrils in disease progression is often unclear.

Purpose of the Study:

To investigate the proteins that co-aggregate with amyloid fibrils within cells.
To identify novel amyloid-forming and amyloid-associated proteins.
To understand the contribution of protein aggregation to cellular degeneration in amyloid diseases.

Main Methods:

Utilized mammalian and yeast model systems.
Employed biophysical properties of amyloid aggregates for purification.
Directly identified proteins within cellular aggregates.

Main Results:

Developed a method to purify and identify proteins directly from cellular aggregates.
Discovered that stress granule components co-aggregate with huntingtin protein fragments.
Identified numerous previously unknown amyloid-associated proteins.

Conclusions:

Amyloid aggregate composition can be stringently analyzed.
Co-aggregation of cellular proteins with amyloid may contribute to disease.
This approach aids in identifying new amyloidogenic proteins and disease mechanisms.