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Self-Assembling Catalytic Peptide Nanomaterials Capable of Highly Efficient Peroxidase Activity.

ABSTRACT: The self-assembly of short peptides gives rise to versatile nanomaterials capable of promoting efficient catalysis. We have shown that short, seven-residue peptides bind hemin to produce functional catalytic materials which display highly efficient peroxidation activity, reaching a catalytic efficiency of 3×10⁵ m^-1 s^-1 . Self-assembly is essential for catalysis as non-assembling controls show no activity. We have also observed peroxidase activity even in the absence of hemin, suggesting the potential to alter redox properties of substrates upon association with the assemblies. These results demonstrate the practical utility of self-assembled peptides in various catalytic applications and further support the evolutionary link between amyloids and modern-day enzymes.

SUBMITTER: Zozulia O

PROVIDER: S-EPMC8208039 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature

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Self-Assembling Catalytic Peptide Nanomaterials Capable of Highly Efficient Peroxidase Activity.

Zozulia Oleksii O Marshall Liam R LR Kim Inhye I Kohn Eric M EM Korendovych Ivan V IV

Chemistry (Weinheim an der Bergstrasse, Germany) 20210226 17

The self-assembly of short peptides gives rise to versatile nanomaterials capable of promoting efficient catalysis. We have shown that short, seven-residue peptides bind hemin to produce functional catalytic materials which display highly efficient peroxidation activity, reaching a catalytic efficiency of 3×105 m-1 s-1 . Self-assembly is essential for catalysis as non-assembling controls show no activity. We have also observed peroxidase activity even in the ab ...[more]

PMID: 33460473

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