ArticleCommunications chemistry2025
A bioinformatics approach to design minimal biomimetic metal-binding peptides.
Article in Communications chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Light-Driven Proton-Coupled Two-Electron Ligand Reduction Causes the Rearrangement of the Coordination Sphere in Cu(I) 4Journal of the American Chemical Society · 2026Article
- A bis-macrocylic peptide ligand mimicking the β-sandwich active site of multicopper oxidases.Dalton transactions (Cambridge, England : 2003) · 2026Article
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9 authors.
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Abstract
Nature-inspired or biomimetic catalysts aim to reach the high catalytic performance and selectivity of natural enzymes while possessing the chemical stability and processability of synthetic catalysts. A promising strategy for designing biomimetic catalysts relies on mimicking the structure of the enzyme active site. This can either entail complicated total synthesis of a synthetic catalyst or design of peptide sequences, able to self-assemble in the presence of metal ions, thus forming metallo-peptide complexes that mimic the active sites of natural enzymes. Using a bioinformatics approach, we designed a minimal peptide made up of eight amino acids (H4pep) to act as a functional mimic of the trinuclear Cu site of the laccase enzyme. Cu(II) binding to H4pep results in the formation of a Cu
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