Hydrogels for Cell Encapsulation and Injectable Delivery via Peptide Folding and Consequent Self-Assembly
University of Delaware, US
peptides, self-assembly, folding, hydrogel, tissue engineering, encapsulation
The local nano- and overall network structure, and resultant viscoelastic and cell-level biological properties, of hydrogels that are formed via ?-hairpin self-assembly will be presented. These peptide hydrogels are potentially ideal scaffolds for tissue repair and regeneration due to their ability to mimic natural extra cellular matrix. The 20 amino acid 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 short fibrils that are 3 nm wide and up to several hundred nm long 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. Importantly, once formed into a solid, self-supporting gel the network can be disrupted by the introduction of a shear stress. The system can shear thin but immediately reheal to preshear stiffness on the cessation of the shear stress.
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Nanotech 2007 Conference Program Abstract