ATP-Regulated Formation of Transient Peptide Amphiphiles Superstructures

Self-assembly of biotic systems serves as inspiration for the preparation of synthetic supramolecular assemblies to mimic the structural, temporal, and functional aspects of living systems. Despite peptide amphiphiles (PAs) being widely studied in the context of biomimetic and bioactive functional nanomaterials, very little is currently known about the reversible and spatiotemporal control of their hierarchical self-assemblies. Here, it is shown that PA-based supramolecular nanofibers can transiently form superstructures, through binding with oppositely charged adenosine triphosphate (ATP), leading to charge screening and stabilization of bundled nanofibers. Enzymatic hydrolysis of ATP to adenosine monophosphate and phosphates causes the disassembly of the superstructures and recovery of individual nanofibers. The lifetime of superstructures can be controlled by adjusting the concentration of either ATP or enzyme. The role that the formation of bundled PA nanofibers has on chemical reactivity and catalysis is also evaluated. It is observed that superstructuration is responsible for downregulation in the PA activity, which can then be recovered by gradual disassembly of the bundles. These results demonstrate the potential of reversible and controlled hierarchical self-assembly to modulate the reactivity and catalysis of peptide nanostructures.