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<p>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<sup>2+</sup>(H4pep)<sub>2</sub> complex with a β-sheet secondary structure, able to reduce O<sub>2</sub>. Our study demonstrates the viability and potential of using short peptides to mimic the minimal functional site of natural enzymes.</p>

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A bioinformatics approach to design minimal biomimetic metal-binding peptides

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2025年10月6日

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  • Claudia Spallacci,
  • Marco Chino,
  • Antonio Rosato,
  • Ornella Maglio,
  • Ping Huang,
  • Luca D’Amario,
  • Angela Lombardi,
  • Claudia Andreini,
  • Mun Hon Cheah

摘要

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 Cu2+(H4pep)2 complex with a β-sheet secondary structure, able to reduce O2. Our study demonstrates the viability and potential of using short peptides to mimic the minimal functional site of natural enzymes.