| Chapter title |
Catalytic Amyloid Fibrils That Bind Copper to Activate Oxygen
|
|---|---|
| Chapter number | 4 |
| Book title |
Synthetic Protein Switches
|
| Published in |
Methods in molecular biology, March 2017
|
| DOI | 10.1007/978-1-4939-6940-1_4 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-6938-8, 978-1-4939-6940-1
|
| Authors |
Alex Sternisha, Olga Makhlynets |
| Editors |
Viktor Stein |
| 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. |
Mendeley readers
Geographical breakdown
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|---|---|---|
| Unknown | 3 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 1 | 33% |
| Student > Bachelor | 1 | 33% |
| Other | 1 | 33% |
| Readers by discipline | Count | As % |
|---|---|---|
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