Short Self-Assembling Peptides Are Able to Bind to Copper and Activate Oxygen

Angew Chem Int Ed Engl. 2016 Jul 25;55(31):9017-20. doi: 10.1002/anie.201602480. Epub 2016 Jun 8.

Abstract

We have shown that de novo designed peptides self-assemble in the presence of copper to create supramolecular assemblies capable of carrying out the oxidation of dimethoxyphenol in the presence of dioxygen. Formation of the supramolecular assembly, which is akin to a protein fold, is critical for productive catalysis since peptides possessing the same functional groups but lacking the ability to self-assemble do not catalyze substrate oxidation. The ease with which we have discovered robust and productive oxygen activation catalysts suggests that these prion-like assemblies might have served as intermediates in the evolution of enzymatic function and opens the path for the development of new catalyst nanomaterials.

Keywords: catalysis; copper; peptides; self-assembly; supramolecular chemistry.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Binding Sites
  • Catalysis
  • Copper / chemistry*
  • Oxygen / chemistry*
  • Peptides / chemical synthesis
  • Peptides / chemistry*

Substances

  • Peptides
  • Copper
  • Oxygen