Differential copper-guided architectures of amyloid β peptidomimetics modulate oxidation states and catalysis

Orchestration of differential architectures of designer peptidomimetics that modulate metal oxidation states to perform multiple chemical transformations remains a challenge. Cu-chelation and self-assembly properties of amyloid beta (A beta 14-23) peptide were tuned by the incorporation of cyclic dipeptide (CDP) and pyrene (Py) as the assembly directing and reporting units, respectively. We explore the molecular architectonics of A beta 14-23 derived peptidomimetics (Akd(NMC)Py) to form differential architectures that stabilize distinct Cu oxidation states. The fibrillar self-assembly of Akd(NMC)Py is modulated to form nanosheets by the one-off addition of Cu-II. Notably, the serial addition of Cu-II resulted in the formation of micelle-like core-shell architectures. The micelle-like and nanosheet architectures were found to differentially stabilize Cu-II and Cu-I states and catalyze tandem oxidative-hydrolysis and alkyne-azide cycloaddition reactions, respectively.

Automated summary

The differential structures of designer peptidomimetics derived from amyloid beta (Aβ14-23) peptide were manipulated to stabilize distinct Cu oxidation states, which catalyzed different chemical reactions effectively. By incorporating cyclic dipeptide (CDP) and pyrene (Py) units, the Cu-chelation and self-assembly properties of Aβ14-23 peptide were tuned to form nanosheets and micelle-like core-shell structures. These structures demonstrated the ability to stabilize Cu-II and Cu-I states separately and catalyze tandem oxidative-hydrolysis and alkyne-azide cycloaddition reactions.