Proteolytic stability of amphipathic peptide hydrogels composed of self-assembled pleated β-sheet or coassembled rippled β-sheet fibrils.

Hydrogel networks composed of rippled β-sheet fibrils of coassembled D- and L-Ac-(FKFE)2-NH2 amphipathic peptides exhibit proteolytic stability and increased rheological strength compared to networks of self-assembled L-Ac-(FKFE)2-NH2 pleated β-sheet fibrils. Modifying the ratios of l and d peptides in the coassembled rippled β-sheet fibrils alters the degradation profiles of these hydrogel networks.