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Bioinspired self-assembly offers a way to create novel functional materials from simple, easy-to-synthesize building blocks. Peptides, in particular, are frequently used in the design of self-assembled materials for their structural properties and the ability for supramolecular ?lock and key? type recognition based on H-bonding networks and dispersion interactions. We have previously reported the head-to-tail self-assembly of N-terminal acetylated ?-peptides into helical fibrils through a supramolecular three point H-bonding motif, and the superstructures formed from inter-fibril interactions. Here we show that the superstructure morphology of a self-assembled ?3-peptide, Ac-?3[LIA], can be tuned to present a range of morphologies by the appropriate solvent medium. From the same monomer we succeeded in creating straight compact ?nano-beams?, self-spun threads and complex, dendritic, hierarchical structures. The variation in geometries is therefore achieved through careful switching and tuning of the relative strengths of the inter-fibril H-bonding, van der Waals and solvophobic interactions.
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