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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,...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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Related Experiment Video

Updated: Oct 6, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Chaperoning shape-shifting tau in disease.

Bryan D Ryder¹, Pawel M Wydorski¹, Zhiqiang Hou²

¹Molecular Biophysics Graduate Program, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Trends in Biochemical Sciences

|January 20, 2022

Summary

Molecular chaperones selectively target toxic protein conformations, like those of tau in neurodegenerative diseases. Understanding this interaction is key to developing new diagnostics and therapies for tauopathies.

Keywords:

Alzheimer’s disease DnaJ amyloid chaperone seeds tau tauopathies

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Area of Science:

Neuroscience
Biochemistry
Structural Biology

Background:

Neurodegenerative diseases, such as Alzheimer's, are linked to protein misfolding.
The microtubule-associated protein tau converts into pathogenic amyloid conformations, driving over 25 tauopathies.
Diverse structural polymorphs of tau amyloid fibrils correlate with distinct disease manifestations.

Purpose of the Study:

To investigate the role of molecular chaperones in regulating tau protein function and aggregation.
To understand how chaperones selectively recognize and interact with different tau conformations.
To explore the implications for developing conformation-specific diagnostic and therapeutic strategies for tauopathies.

Main Methods:

Structural analysis of tau amyloid fibrils isolated from human tauopathy tissues.
Biochemical assays to study chaperone-protein interactions.
Cellular models to investigate chaperone-mediated regulation of tau aggregation.

Main Results:

Tau protein adopts diverse structural polymorphs in different tauopathies.
Molecular chaperones selectively recognize specific tau conformations.
Chaperones play a crucial role in limiting the accumulation of proteotoxic tau species.

Conclusions:

Chaperone-mediated recognition of distinct tau conformations is a critical mechanism in neurodegenerative disease.
Targeting chaperone-tau interactions offers potential for novel, conformation-specific therapies.
Further research is needed to elucidate chaperone influence across various tauopathies for improved diagnostics and treatments.