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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: Mar 21, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Efficient synthesis of longer Aβ peptides via removable backbone modification.

Chao Zuo¹, Shan Tang, Yan-Yan Si

¹High Magnetic Field Laboratory, Chinese Academy of Sciences, School of Life Sciences, University of Science and Technology of China, Hefei 230026, China. jszheng@hmfl.cas.cn.

Organic & Biomolecular Chemistry

|May 19, 2016

Summary

This summary is machine-generated.

Synthesizing longer amyloid-beta (Aβ) peptides for Alzheimer's disease (AD) research is now more efficient. A new chemical strategy simplifies the preparation and purification of these crucial Aβ peptides.

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Area of Science:

Neuroscience
Biochemistry
Organic Chemistry

Background:

Longer amyloid-beta (Aβ) peptides (43-49 amino acids) are implicated in Alzheimer's disease (AD) pathology.
The chemical synthesis of these longer Aβ peptides presents significant challenges, hindering research into their specific roles in AD.

Purpose of the Study:

To develop a robust and efficient chemical synthesis strategy for longer amyloid-beta (Aβ) peptides, specifically Aβ48 and Aβ49.
To overcome the obstacles in preparing and characterizing these longer Aβ peptides for improved Alzheimer's disease research.

Main Methods:

A novel chemical synthesis approach was employed for longer Aβ peptides.
A key innovation involved incorporating removable Arg4-tagged backbone modification groups within the hydrophobic region of Aβ.

Main Results:

The developed method facilitates improved handling properties during purification, ligation, and mass characterization of longer Aβ peptides.
Successful synthesis of Aβ48 and Aβ49 peptides demonstrates the practicality and efficiency of the new strategy.

Conclusions:

This new chemical synthesis strategy provides a reliable method for producing longer Aβ peptides.
The improved synthesis and handling properties will advance the study of amyloid-beta's role in Alzheimer's disease pathogenesis.