Sternisha Alex, Makhlynets Olga
Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Methods Mol Biol. 2017;1596:59-68. doi: 10.1007/978-1-4939-6940-1_4.
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.
由从头设计的肽组装而成的淀粉样纤维以类似于金属酶通过折叠提供适当配位环境的方式，将配体锁定在对金属结合和催化最佳的构象中。这些超分子组装体在锌存在下有效地催化对硝基苯酯水解，在铜存在下通过双氧催化苯酚氧化。所得的多相催化剂本质上是可切换的，因为金属离子的添加和去除分别开启和关闭催化活性。肽制备和自组装的简便性使淀粉样纤维成为开发用于广泛化学反应的催化剂的有吸引力的平台。在这里，我们展示了制备含铜纤维及其氧化苯酚能力的动力学表征的详细方案。
