This work explains why and how heterochiral and homochiral tripeptides differ in their assembly in water. A characteristic spectroscopic signature is assigned to molecular conformation. We monitor the process as a continuum from the molecular scale to the macroscopic biomaterials so that the final properties are linked to chemical structure of the building blocks. This work lays the foundation for the design of supramolecular hydrogel biomaterials based on short sequences of hydrophobic D-and L-amino acids.
Change of chirality of the first N-terminal amino acid of tripeptides VFF and FFV from l to d results in self-assembled hydrogels at physiological pH from non-assembling l-analogues. Interestingly, changing the chirality of F yields very different nanostructures; nanotapes are observed for (D)VFF, twisted fibers for (D)FFV.
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