Short Self-Assembling Peptides Are Able to Bind to Copper and Activate Oxygen.
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.
Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Olga V
OV
Makhlynets
Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Pallavi M
PM
Gosavi
Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA. ikorendo@syr.edu.
Ivan V
0000-0001-8144-783X
IV
Korendovych
D001665:Binding Sites; D002384:Catalysis; D003300:Copper / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*
D010455:Peptides; D003300:Copper; D010100:Oxygen
catalysis; copper; peptides; self-assembly; supramolecular chemistry