Abstract
Amyloid-like fibrils assembled from de novo designed peptides lock ligands in a conformation optimal for metal binding and catalysis in a manner similar to how metalloenzymes provide proper coordination environment through fold. These supramolecular assemblies efficiently catalyze p-nitrophenyl ester hydrolysis in the presence of zinc and phenol oxidation by dioxygen in the presence of copper. The resulting heterogeneous catalysts are inherently switchable, as addition and removal of the metal ions turns the catalytic activity on and off, respectively. The ease of peptide preparation and self-assembly makes amyloid-like fibrils an attractive platform for developing catalysts for a broad range of chemical reactions. Here, we present a detailed protocol for the preparation of copper-containing fibrils and for kinetic characterization of their abilities to oxidize phenols.
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Acknowledgment
This work was supported in part by the NSF ADVANCE (HRD-1008643) fellowship to O.V.M.
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Sternisha, A., Makhlynets, O. (2017). Catalytic Amyloid Fibrils That Bind Copper to Activate Oxygen. In: Stein, V. (eds) Synthetic Protein Switches. Methods in Molecular Biology, vol 1596. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6940-1_4
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DOI: https://doi.org/10.1007/978-1-4939-6940-1_4
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