Hydrogels have been widely explored for use as materials in assorted biomedical applications, including as tissue engineering scaffolds, antifouling surfaces, and drug delivery vehicles. A number of peptides have been reported to self-assemble into robust hydrogels via inter-strand crosslinking. However, peptide-based materials pose practical and clinical challenges as a result of their susceptibility to proteolytic degradation and the relative difficulty associated with chemical functionalization of their side chains. Here, we present a series of polymer mimics of one particular peptide that forms hydrogels by a combination of electrostatic and hydrophobic interactions as a result of the repeating Lys-Leu-Asp-Leu units that comprise its sequence. In our design, analogues of these amino acids are prepared as modified norbornene monomers and polymerized by ring opening metathesis polymerization (ROMP). With this strategy, the peptide backbone is replaced with a norbornene backbone that is resistant to proteolytic degradation and can be easily modified to include a wide range of chemical functionality. In this work, we present a comparison between the physical properties of our polymer mimics to those of the parent peptide and describe intriguing variations whose gelation can be controlled by changes in solution salt concentration.

Amino acid-modified norbornyl polymers as analogues to hydrogel-forming peptides

251st National Meeting (2016)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.