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

Abstract

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.