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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: Oct 15, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

When aggregation-induced emission meets protein aggregates.

Sicheng Tang¹, Songtao Ye¹, Xin Zhang¹

¹Department of Chemistry.

National Science Review

|October 25, 2021

Summary

This summary is machine-generated.

New research tools called AIEgens (aggregation-induced emission materials) can now monitor protein aggregation in real-time within cells. This breakthrough aids in understanding and potentially treating diseases linked to protein misfolding.

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Last Updated: Oct 15, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Protein aggregation is implicated in numerous human diseases.
Current research tools lack the ability to monitor this process in live cells.
There is a critical need for advanced methods to study protein aggregation dynamics.

Purpose of the Study:

To introduce and evaluate novel research tools for monitoring protein aggregation.
To demonstrate the utility of AIEgens in observing protein aggregation in real-time.
To highlight the potential of AIEgens for disease diagnosis and treatment.

Main Methods:

Development and application of aggregation-induced emission materials (AIEgens).
In vitro studies of protein aggregation using AIEgens.
In vivo studies monitoring protein aggregation within live cells.

Main Results:

AIEgens successfully monitored the entire protein aggregation process.
Real-time observation of protein aggregation was achieved in both test tubes and live cells.
The developed AIEgens show high sensitivity and specificity for protein aggregates.

Conclusions:

AIEgens represent a significant advancement in research tools for studying protein aggregation.
These tools offer unprecedented insights into the mechanisms of protein misfolding diseases.
Future applications of AIEgens are promising for disease diagnostics and therapeutic strategies.