A visible light initiated thiol-acrylate photopolymerization scheme was used to synthesize dually degradable PEG-peptide hydrogels. We evaluated the effect of immobilized mono-thiol pendent peptide on gel crosslinking and presented methods to tune hydrogel crosslinking, including adjusting co-monomer concentration or using multifunctional peptide crosslinker. Specifically, gel stiffness was reduced when mono-thiol peptides were immobilized in the network (Fig 1A-B). Increasing co-monomer concentration (Fig 1C) or by using multi-thiol peptide linker improved the stiffness of the hydrogels. The thioether ester bonds formed after gel crosslinking render the gels hydrolytically labile (Fig 1D). No significant difference was found between different formulations though the groups with greater total thiol or RGDS concentration degraded slightly faster. If the di-thiol peptide linkers are sensitive to proteases, the thiol-acrylate hydrogels can also undergo partial proteolysis (Fig 1E). The thiol-acrylate PEG-peptide hydrogels have tunable stiffness and integrin ligand presentation, which permits the study of hepatic cancer cell fate <i>in vitro</i>. Current work is focused on characterizing the influence of matrix stiffness and integrin signaling on the activation of the HIPPO pathway.

Designing visible light cured thiol-acrylate hydrogels for studying cell fate processes in 3D

251st National Meeting (2016)

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