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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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Updated: Aug 22, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Catalytically Active Amyloids as Future Bionanomaterials.

Rodrigo Diaz-Espinoza¹

¹Departamento de Biología, Facultad de Química y Biología, Universidad de Santiago de Chile, Santiago 3363, Chile.

Nanomaterials (Basel, Switzerland)

|November 11, 2022

Summary

Researchers are developing self-assembling peptide amyloids with unique mechanical and catalytic properties. These protein-based nanomaterials mimic enzymes and show promise for future bionanomaterial applications.

Keywords:

amyloids catalysis cofactors enzymes esterase nanomaterials peptides phosphoesterase redox

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Area of Science:

Biomaterials Science
Supramolecular Chemistry
Nanotechnology

Background:

Peptides and proteins self-assemble into amyloid structures.
Amyloids feature intermolecular beta sheets, forming fibrillary architectures with unique mechanical properties.
These properties are suitable for developing novel nanomaterials.

Purpose of the Study:

To summarize the development of catalytically active amyloids.
To highlight hydrolysis-mediated catalytic activities.
To discuss novel catalytic activities and their potential.

Main Methods:

Rational design of peptide sequences for self-assembly into amyloids.
Investigation of amyloid structures and their reactive surfaces.
Review of reported catalytic activities, focusing on hydrolysis.

Main Results:

Designed peptide sequences self-assemble into catalytically active amyloids.
Amyloids exhibit reactive surfaces mimicking enzyme active sites.
Hydrolysis-mediated activities are well-studied, with novel activities emerging.

Conclusions:

Catalytically active amyloids combine mechanical and catalytic functions.
Potential for developing future bionanomaterials for specific applications.
Amyloid scaffolds offer a promising platform for enzyme-mimicking catalysts.