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Short Self‐Assembling Peptides Are Able to Bind to Copper and Activate Oxygen
Author(s) -
Makhlynets Olga V.,
Gosavi Pallavi M.,
Korendovych Ivan V.
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201602480
Subject(s) - supramolecular chemistry , catalysis , chemistry , substrate (aquarium) , self assembly , copper , combinatorial chemistry , peptide , nanomaterials , oxygen , biophysics , nanotechnology , biochemistry , materials science , organic chemistry , biology , molecule , ecology
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.