Chymotrypsin is a digestive enzyme that breaks down proteins and polypeptides. In this project α-chymotrypsin was modified with well-defined oligomers synthesized by reversible addition-fragmentation chain transfer (RAFT). RAFT was selected due to broad functional group tolerance. Two well defined oligomers were synthesized from the monomers N,N-dimethylacrylamide (DMAm) and oligo(ethylene oxide) methyl ether acrylate (OEOA). Oligomers of DMAm were synthesized with molecular weights of 1000 (DP=10) and 5000 (DP=50) and an oligomer of OEOA was synthesized with molecular weight of 5000 (DP=10). The polymers were conjugated to the free amine groups of chymotrypsin through coupling, with 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide and N-Hydroxysuccinimide (EDC/NHS). The protein-polymer conjugates retained enzymatic activity and the high molecular weight DMAm and the OEOA based conjugates showed significantly improved stability over time compared to the native enzyme. This increase in stability is likely due to the polymer preventing autolysis.

Why synthesize protein–polymer conjugates? The stability and activity of chymotrypsin-polymer bioconjugates synthesized by RAFT

251st National Meeting (2016)

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