ArticleNature materials2021
Cofactor-free oxidase-mimetic nanomaterials from self-assembled histidine-rich peptides.
Article in Nature materials, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 139 citations in OpenAlex.
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- Emergent properties of supramolecular peptide assemblies.Chemical communications (Cambridge, England) · 2026Review
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- Inflammation-free electrochemical in vivo sensing of dopamine with atomic-level engineered antioxidative single-atom catalyst.Nature communications · 2024Article
- Nitrite reductase-mimicking catalysis temporally regulating nitric oxide concentration gradient adaptive for antibacterial therapy.Science advances · 2024Article
- A Cost-Effective Hemin-Based Artificial Enzyme Allows for Practical Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Natural oxidases mainly rely on cofactors and well-arranged amino acid residues for catalysing electron-transfer reactions but suffer from non-recovery of their activity upon externally induced protein unfolding. However, it remains unknown whether residues at the active site can catalyse similar reactions in the absence of the cofactor. Here, we describe a series of self-assembling, histidine-rich peptides, as short as a dipeptide, with catalytic function similar to that of haem-dependent peroxidases. The histidine residues of the peptide chains form periodic arrays that are able to catalyse H
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