Abstract
Protein amyloids generally constitute β-sheet rich fibrillar assemblies. Amyloid fibrils have been identified in varied diseases, formed by bacterially secreted proteins, and generated in de novo designed peptides. This review article summarizes the burgeoning body of work reporting catalytic properties of amyloid fibrils. We highlight representative studies focusing on catalytic amyloid peptides, both synthetic and naturally occurring. We discuss the structural features associated with catalysis and putative catalytic sites on amyloid fibrils’ surfaces. We also highlight studies demonstrating catalytic functions of short amyloid-like sequences and their possible involvement in early-life reactions, acting as primitive enzymes. Finally, we discuss recent reports of the catalytic activities of native amyloids, pointing to possible roles of amyloid catalysis in disease progression and pathologies.
| Original language | English |
|---|---|
| Pages (from-to) | 907-917 |
| Number of pages | 11 |
| Journal | Trends in Chemistry |
| Volume | 4 |
| Issue number | 10 |
| DOIs | |
| State | Published - 1 Oct 2022 |
Keywords
- amyloids
- catalytic amyloids
- catalytic peptides
- fibrils
ASJC Scopus subject areas
- General Chemistry
Fingerprint
Dive into the research topics of 'Catalytic amyloids'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver