Abstract
A nonapeptide, which is sensitive to enzymatic digestion by collagenase, was modified by the covalent attachment of an acrylamido group at the terminal positions. The functionalized peptide was used as a crosslinking agent during polymerization of 2-hydroxyethyl methacrylate (HEMA). Reversible addition-fragmentation chain transfer (RAFT) method was used to obtain a polymer (PHEMA) with an average theoretical molecular weight of 4000 Da, containing enzymatically labile peptide crosslinks. The functionalized peptide was analyzed in detail by 1H and 13C nuclear magnetic resonance (NMR) spectrometry. The polymerization reaction was monitored by near infrared spectrometry, while the resulting polymer was analyzed by size exclusion chromatography and solid NMR spectrometry. The peptide-crosslinked PHEMA was subjected to an in-vitro degradation assay in the presence of collagenase. At the highest concentration of enzyme used in the study, a weight loss of 35% was recorded after 60 days of incubation in the collagenolytic medium. This suggests that crosslinking with enzymatically degradable peptides is a valid method for inducing biodegradability in polymers that otherwise are not degradable.
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