Abstract
The dipeptide, fluorenylmethyloxycarbonyl- di- phenylalanine (FmocFF), has displayed the self-assembly characteristics of short peptides in a way to induce hydrogel formation. The biocompatibility of these hydrogels makes them an important material to study. The underlying fibrils of the gel phase are built of β-sheets stabilized by ππ stacking between respective aromatic side chains and end group of the peptide. Gel formation can be triggered by adding water to dimethysulfoxide or by dissolving the peptide at a pH greater than 10.0 and subsequently titrating with HCl.
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