Catalytic amyloid fibrils that bind copper to activate oxygen

Alex Sternisha, Olga Makhylnets

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations

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.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages59-68
Number of pages10
Volume1596
DOIs
StatePublished - Jan 1 2017

Publication series

NameMethods in Molecular Biology
Volume1596
ISSN (Print)1064-3745

Keywords

  • Catalysis
  • Dioxygen activation
  • Fibrils
  • Peptides
  • Phenol oxidation

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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    Sternisha, A., & Makhylnets, O. (2017). Catalytic amyloid fibrils that bind copper to activate oxygen. In Methods in Molecular Biology (Vol. 1596, pp. 59-68). (Methods in Molecular Biology; Vol. 1596). Humana Press Inc.. https://doi.org/10.1007/978-1-4939-6940-1_4