Self-assembled Beta-hairpin Peptides- responsive Gels and Templates for Hybrid Materials

摘要

The local nano- and overall network structure, and resultant viscoelastic and cell-level biological properties, of hydrogels that are formed via β-hairpin self-assembly will be presented. These peptide hydrogels are potentially excellet scaffolds for tissue repair and regeneration due to inherent cytocompatibility, porous morphology, and shear-thinning but instant recovery viscoelastic properties. The 20 amino acid parent peptide MAX1 (H2N-VKVKVKVKVDPPTKVKVKVKV- CONH2), has been shown to fold and self-assemble into a rigid hydrogel based on environmental cues such as pH, salt, and temperature including physiological conditions. The hydrogel is composed of a network of fibrils that are 3 nm wide and heavily branched and entangled with no covalent crosslinking required for gel stiffness. In addition, slight design variations of the MAX1 sequence allow for tunability of the self-assembly/hydrogelation kinetics. In turn, by controlling hydrogel self-assembly kinetics, one dictates the ultimate stiffness of the resultant network and the kinetics through which gelation occurs.