ArticleChembiochem : a European journal of chemical biology2025
Exploiting SpyTag/SpyCatcher Technology to Design New Artificial Catalytic Copper Proteins.
Article in Chembiochem : a European journal of chemical biology, 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.
- Fabrication of a 3D nano-bienzyme cascade reactor based on a Dps protein scaffold for chiral amine synthesis.Bioresources and bioprocessing · 2026Article
- Stability and Pseudocatecholase Activity of Artificial Bis-Histidyl Copper Peptides.Inorganic chemistry · 2025Article
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Authors and funding
12 authors.
Funding
Abstract
Designing artificial metal binding sites within a protein is challenging since amino acid residues need to be placed in desired positions in the final construct and the use of non-natural amino acids is difficult. The alternative approach of directing the insertion of artificial metal coordination systems presents the difficulty of grafting such site in a single desired position. Spy protein is composed of a protein component (SpyCatcher) which binds spontaneously an oligopeptide (SpyTag) with formation of an isopeptide bond. A SpyTag peptide equipped with an ATCUN (amino terminal copper and nickel) binding site is designed to bind copper(II) with high femtomolar affinity both in the absence of SpyCatcher and in the reconstituted Spy construct. The Cu
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