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

Hydrogel networks composed of rippled beta-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 beta-sheet fibrils. Modifying the ratios of L and D peptides in the coassembled rippled beta-sheet fibrils alters the degradation profiles of these hydrogel networks.