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We use a range of spectroscopic methods to provide mechanistic insight into a phosphatase-driven supramolecular transformation whereby an amphiphilic peptide building block, upon dephosphorylation, switches from a solution-phase, micellar structure to a gel-phase, chiral uni-directional nanofibre morphology.

Self-assembled peptide systems have been widely studied in the context of gaining understanding of the rules that govern biomolecular processes and increasingly as new bio-inspired nanomaterials. Such materials may be designed to be highly dynamic, displaying adaptive and self-healing properties. This review focuses on recent approaches, which exploit reversible covalent and noncovalent chemistry in combination with peptide-based self-assembly. Selected examples of recent advances include sulphur and nitrogen-based reversible reactions, metal-ligand coordination and enzyme-assisted transamidation that lead to structures such as catenanes, nanofibres, β-hairpins and coiled-coil assemblies. It is demonstrated that these structures give rise to nanomaterials with emergent properties that are highly sensitive and adaptive to external conditions and may allow for in vitro evolution of novel peptide nanostructures via templating or self-recognition., (Copyright © 2010 Elsevier Ltd. All rights reserved.)

We describe an enzyme-driven dynamic supramolecular peptide system which displays multiple reversible pathways, giving rise to emergent properties that are dictated by environmental conditions and that can be locked in a gel-state.