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Updated: Oct 23, 2025

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Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
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Catalytic amyloids: Is misfolding folding?
Liam R Marshall1, Ivan V Korendovych1
1Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
Current Opinion in Chemical Biology
|August 23, 2021
Summary
Amyloids, once seen as disease-related, are now recognized for beneficial functions as
Area of Science:
- Biochemistry
- Biotechnology
- Materials Science
Background:
- Amyloids were traditionally viewed as pathological aggregates.
- Emerging evidence highlights diverse, beneficial biological roles of amyloids.
- Amyloid structures represent an 'alternative folding' rather than 'misfolding'.
Purpose of the Study:
- To summarize recent advancements in catalytic amyloids.
- To review applications of de novo and bioinspired catalytic amyloids.
- To discuss the field's progress over the last two years.
Main Methods:
- Literature review of recent developments in catalytic amyloids.
- Analysis of de novo and bioinspired amyloid catalyst designs.
- Synthesis of recent findings on amyloid catalysis.
Main Results:
- Amyloid folds can be engineered into highly efficient catalysts.
- These catalytic amyloids exhibit enzyme-like efficiencies.
- Diverse applications showcase the potential of engineered amyloid catalysts.
Conclusions:
- The perception of amyloids has shifted from disease markers to functional biomaterials.
- Catalytic amyloids offer a promising platform for novel biocatalysis.
- Continued research is expanding the utility and understanding of amyloid structures.
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