| Literature DB >> 33460473 |
Oleksii Zozulia1, Liam R Marshall1, Inhye Kim1, Eric M Kohn1, Ivan V Korendovych1.
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.Entities:
Keywords: amyloids; enzyme catalysis; peptides; peroxidases; self-assembly
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Year: 2021 PMID: 33460473 PMCID: PMC8208039 DOI: 10.1002/chem.202100182
Source DB: PubMed Journal: Chemistry ISSN: 0947-6539 Impact factor: 5.236