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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.
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Mutations

Mutations

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Related Experiment Video

Updated: Jul 9, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation.

Kerry T Sun¹, Tark Patel¹, Sang-Gyun Kang¹

¹Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.

ACS Chemical Neuroscience

|December 6, 2023

Summary

This summary is machine-generated.

Disease-associated mutations in tau protein can alter the structure of tau fibrils, impacting their assembly. These findings shed light on the molecular mechanisms underlying tauopathies and neurodegenerative diseases.

Keywords:

aggregation kinetics disease mutations protein conformation proteolysis tau aggregation tauopathies

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

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An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

Published on: May 23, 2019

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Tau protein accumulation into fibrils is a hallmark of neurodegenerative diseases known as tauopathies.
Distinct tau fibril structures are observed in different tauopathies, identified via cryo-electron microscopy (cryo-EM).
Some tauopathies are linked to mutations in the tau protein, but their effect on fibril structure remains unclear.

Purpose of the Study:

To investigate whether missense mutations in the tau protein influence the structure of tau fibrils.
To understand the impact of tau mutations on fibril assembly and structure.

Main Methods:

Development of a high-throughput platform for purifying 37 full-length 0N4R tau variants.
In vitro fibril formation using purified tau variants.
High-throughput protease sensitivity platform to analyze relative fibril structures.

Main Results:

A subset of disease-associated tau mutations formed fibrils similar to wild-type tau.
Other mutations resulted in strikingly different fibril structures compared to wild-type.
Mutation location and assembly kinetics did not clearly predict the impact on tau structure.

Conclusions:

Single-point mutations in tau can significantly alter fibril assembly and structure.
Tau mutations impact fibril core structures via complex molecular mechanisms.
These findings provide insights into tau's role in disease pathology and the development of tauopathies.