Assembly and catalytic activity of short prion-inspired peptides.
Methods Enzymol
; 697: 499-526, 2024.
Article
in En
| MEDLINE
| ID: mdl-38816134
ABSTRACT
Enzymes play a crucial role in biochemical reactions, but their inherent structural instability limits their performance in industrial processes. In contrast, amyloid structures, known for their exceptional stability, are emerging as promising candidates for synthetic catalysis. This article explores the development of metal-decorated nanozymes formed by short peptides, inspired by prion-like domains. We detail the rational design of synthetic short Tyrosine-rich peptide sequences, focusing on their self-assembly into stable amyloid structures and their metallization with biologically relevant divalent metal cations, such as Cu2+, Ni2+, Co2+ and Zn2+. The provided experimental framework offers a step-by-step guide for researchers interested in exploring the catalytic potential of metal-decorated peptides. By bridging the gap between amyloid structures and catalytic function, these hybrid molecules open new avenues for developing novel metalloenzymes with potential applications in diverse chemical reactions.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Prions
Language:
En
Journal:
Methods Enzymol
/
Methods enzymol
/
Methods in enzymology
Year:
2024
Document type:
Article
Country of publication:
United States