Enzyme-induced peptide hydrogelation provides a sensitive method for scaffold assembly in response to changes in biological environments. Geling peptides bearing a substrate for the inflammatory related enzymes, matrix metalloproteinase (MMP)-2/9, were cyclized via disulfide bonds to create a water-soluble pro-gelator. When enzymatically cleaved, sterically strained cyclic peptides linearize and self-assemble via beta-sheets into hydrogels, as shown by TEM, rheometry, and circular dichroism. Furthermore, incorporation of various functional ligands does not disrupt hydrogel assembly. These initial studies set the stage for the development of targeting systems for therapeutic hydrogel delivery to inflammation-associated diseases.

Enzyme responsive pro-geling cyclic peptides

251st National Meeting (2016)

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