De Novo Design of a Self-Assembled Artificial Copper Peptide that Activates and Reduces Peroxide.

ABSTRACT: Copper-containing metalloenzymes constitute a major class of proteins which catalyze a myriad of reactions in nature. Inspired by the structural and functional characteristics of this unique class of metalloenzymes, we report the conception, design, characterization, and functional studies of a de novo artificial copper peptide (ArCuP) within a trimeric self-assembled polypeptide scaffold that activates and reduces peroxide. Using a first principles approach, the ArCuP was designed to coordinate one Cu via three His residues introduced at an a site of the peptide scaffold. X-ray crystallographic, UV-vis and EPR data demonstrate that Cu binds via the N_ε atoms of His forming a T2Cu environment. When reacted with hydrogen peroxide, the putative copper-hydroperoxo species is

SUBMITTER: Mitra S 

PROVIDER: S-EPMC9524465 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature