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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,...

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Related Experiment Video

Updated: Jun 3, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Heterotypic Seeding Generates Mixed Amyloid Polymorphs.

Siddhartha Banerjee¹, Divya Baghel¹, Harrison O Edmonds¹

¹Department of Chemistry and Biochemistry, The University of Alabama, 1007E Shelby Hall, Tuscaloosa, AL 35487, USA.

|January 9, 2025

Summary

This summary is machine-generated.

Amyloid beta (Aβ) can form abnormal aggregates with other proteins, leading to altered structures in Alzheimer's disease (AD). Understanding these complex interactions is key for developing new AD therapies.

Keywords:

Alzheimer’s disease amyloid beta atomic force microscopy-integrating infrared infrared spectroscopy nanoscale spectroscopy protein aggregation

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Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

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Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Published on: March 16, 2016

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Last Updated: Jun 3, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

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Published on: June 2, 2019

Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Intracerebroventricular Injection of Amyloid-β Peptides in Normal Mice to Acutely Induce Alzheimer-like Cognitive Deficits

Published on: March 16, 2016

Area of Science:

Biochemistry
Neuroscience
Molecular Biology

Background:

Amyloid beta (Aβ) fibril formation is central to Alzheimer's disease (AD) pathogenesis.
The influence of structurally diverse seeds on Aβ aggregation remains incompletely understood.
Investigating heterotypic aggregation is crucial for understanding AD complexity.

Purpose of the Study:

To investigate how structurally different seeds affect amyloid beta (Aβ) aggregate structure.
To explore the formation of heterotypic amyloid aggregates.
To understand the implications for Alzheimer's disease (AD) pathology.

Main Methods:

Nanoscale infrared spectroscopy was employed to analyze individual amyloid aggregates.
Amyloid beta (Aβ) was aggregated with specific antiparallel fibrillar seeds.
Coaggregation experiments included Aβ isomers, alpha-synuclein, and brain protein lysates.

Main Results:

Amyloid beta (Aβ) formed heterotypic or mixed polymorphs with altered structures when seeded.
These heterotypic aggregates deviated from the typical parallel cross-β conformation.
Heterotypic fibril formation extended beyond Aβ isomers to include alpha-synuclein and brain lysates.

Conclusions:

Amyloid beta (Aβ) aggregation in Alzheimer's disease (AD) is more complex than previously thought.
Heterotypic interactions significantly alter amyloid aggregate structure.
Further research into Aβ interactions with other brain components is vital for therapeutic development.