| The challenge of developing materials that can emulate the material strength and stability of natural tissues is addressed through the implementation of a strategy to enhance the mechanical properties of a self-assembling peptide-hydrogel. MAX1, a peptide having the sequence VKVKVKVKVDPPTKVKVKVKV-NH 2, has been shown to self-assemble into a beta-sheet-rich structure forming a non-covalently crosslinked fibrillar network. However, at low peptide concentrations and physiological conditions, imparting additional crosslinks in the gel to produce a more rigid network is desirable. Studies were performed where a crosslinking agent, genipin (GP), was added to a 1 wt% MAX1 hydrogel. GP is capable of reacting with primary amines and, thus, can form covalent crosslinks between MAX1 fibrils by reacting with the lysine side-chains and imparting more crosslinks into the material. The effect of the crosslinking agent on beta-sheet formation and the elastic modulus of the MAX1 hydrogels was studied, and enhanced rigidity was observed for hydrogels with GP crosslinkages. Moreover, the time at which GP is added during the peptide folding and self-assembly process was determined to have an effect on the resultant hydrogel formed and the corresponding material properties. |
