ACS Appl Mater Interfaces. 2026 Mar 27. doi: 10.1021/acsami.6c03253. Online ahead of print.

ABSTRACT

Laccases, a typical metalloenzyme, catalyze the oxidation of organic substrates while reducing molecular oxygen to water. Reconstructing the in-between states (IBS) of the laccase active site is essential for understanding its catalytic mechanism and for guiding artificial enzyme design. In this study, we designed a peptide-metal coassembly using amyloid peptides with copper ions, forming stable and ordered structures. Structural characterization confirms β-sheet formation stabilized by Cu²⁺ coordination, providing a robust framework for catalysis. Computational analysis reveals the copper coordination geometry and catalytic electronic properties, demonstrating the realization of the key IBS at the active site of the assembly. Subsequent experimental validation confirms the significant laccase-like activity of the peptide-metal coassemblies even under challenging conditions of varying pH, temperature, and prolonged storage. This highlights their resilience and sustained catalytic efficiency, making them promising candidates for industrial and environmental applications. This study provides a comprehensive understanding of peptide-metal coassemblies as laccase mimetics, laying the groundwork for the rational design of more efficient and versatile catalytic systems for industrial and environmental applications.

PMID:41891543 | DOI:10.1021/acsami.6c03253