ArticleSmall (Weinheim an der Bergstrasse, Germany)2025
ATP-Regulated Formation of Transient Peptide Amphiphiles Superstructures.
Article in Small (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Transient Salt-Bridge-Based Supramolecular Polymers: Experiments and Theory.Journal of the American Chemical Society · 2026Article
- Molecular Engineering of Recombinant Protein Hydrogels: Programmable Design and Biomedical Applications.Gels (Basel, Switzerland) · 2025Review
- ATP-Regulated Formation of Transient Peptide Amphiphiles Superstructures.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
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