Differential copper-guided architectures of amyloid β peptidomimetics modulate oxidation states and catalysis. Issue 9 (19th April 2022)

• Record Type: Journal Article
• Authors: Ghosh, Debasis; Konar, Mouli; Mondal, Tanmay; Govindaraju, Thimmaiah
• Is Part Of: Nanoscale advances. Volume 4:Issue 9(2022)
• Page Start: 2196
• Page End: 2200
• Publication Date: 2022-04-19
• Subjects: 620.5
• DOI: 10.1039/d2na00161f
• Languages: English
• ISSNs: 2516-0230

Abstract

Abstract : The fibrillar assembly of Akd NMC Py peptidomimetics with cyclic dipeptide and pyrene units was engineered into Cu-guided differential architectures that stabilize Cu II and Cu I states and exhibit distinct catalytic activities. Abstract : 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 β (Aβ14-23) 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 Aβ14-23 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.