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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: Jul 4, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Local structural preferences in shaping tau amyloid polymorphism.

Nikolaos Louros^1,2, Martin Wilkinson³, Grigoria Tsaka^1,2

¹Switch Laboratory, VIB Center for Brain and Disease Research, Herestraat 49, 3000, Leuven, Belgium.

Nature Communications

|February 3, 2024

Summary

This summary is machine-generated.

Researchers discovered a new tau protein segment, PAM4 (Polymorphic Amyloid Motif of Repeat 4), crucial for forming diverse amyloid structures in tauopathies. This finding explains how different tau strains propagate in neurodegenerative diseases like Alzheimer's.

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In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

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Published on: November 20, 2018

Area of Science:

Neuroscience
Biochemistry
Structural Biology

Background:

Tauopathies are neurodegenerative diseases defined by varied tau amyloid fibril structures.
The underlying reasons for tau polymorphism across different diseases are not fully understood.
Intrinsic structural properties of tau amyloid cores may influence fibril polymorphism.

Purpose of the Study:

To identify intrinsic structural elements contributing to tau amyloid fibril polymorphism.
To investigate the role of these elements in tau propagation within neurodegenerative diseases.

Main Methods:

Experimental identification of a novel amyloidogenic motif, PAM4 (Polymorphic Amyloid Motif of Repeat 4).
Computational analysis of per-residue contributions to fibril core stability.
Cryo-electron microscopy (cryo-EM) of synthetic PAM4 peptide fibrils.
In-cell experiments assessing the seeding efficiency of tau aggregates with and without PAM4.

Main Results:

A new motif, PAM4, was identified as a significant contributor to tau polymorphism.
PAM4 plays a key role in maintaining structural integrity across different amyloid polymorphs.
Synthetic PAM4 peptides formed structures mimicking disease-associated tau strains.
Deletion of PAM4 reduced the cellular seeding efficiency of tau aggregates from Alzheimer's disease, corticobasal degeneration, and progressive supranuclear palsy.

Conclusions:

Intrinsic structural propensities of amyloid core segments, like PAM4, dictate tau structure in cells.
PAM4 is pivotal in the propagation of tau amyloid structures in tauopathies.
Understanding PAM4's role offers insights into the molecular mechanisms driving neurodegeneration.