Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 27, Issue 17, Pages 5388-5392Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.202100182
Keywords
amyloids; enzyme catalysis; peptides; peroxidases; self-assembly
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Funding
- NIH [GM119634]
- CRDF [OISE-18-63891-0]
- Alexander von Humboldt Foundation
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Self-assembly of short peptides can produce versatile nanomaterials with efficient catalytic activity, showing practical utility and evolutionary connection.
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 3x10(5) 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.
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