Why synthesize protein–polymer conjugates? The stability and activity of chymotrypsin-polymer bioconjugates synthesized by RAFT. (18th August 2015)

• Record Type: Journal Article
• Authors: Falatach, Rebecca; Li, Shaohua; Sloane, Samantha; McGlone, Cameron; Berberich, Jason A.; Page, Richard C.; Averick, Saadyah; Konkolewicz, Dominik
• Is Part Of: Polymer. Volume 72(2015)
• Page Start: 382
• Page End: 386
• Publication Date: 2015-08-18
• Subjects: RAFT polymerization -- Controlled radical polymerization -- Protein–polymer conjugate; Polymers -- Periodicals; Polymerization -- Periodicals; Polymères -- Périodiques; Polymérisation -- Périodiques; 547.7
• DOI: 10.1016/j.polymer.2015.04.010
• Languages: English
• ISSNs: 0032-3861

Abstract

Abstract: α-Chymotrypsin, a commonly used protease, was modified with well-defined oligomers synthesized by RAFT. The well defined polymers were synthesized based on the monomers N, N-dimethylacrylamide (DMAm) or oligo(ethylene oxide) methyl ether acrylate (OEOA). The polymers were conjugated to free amine groups on chymotrypsin through an in-situ 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide/ N -hydroxysuccinimide (EDC/NHS) coupling approach. The protein–polymer conjugates retained enzymatic activity, and the higher molecular weight DMAm and OEOA polymer, created protein–polymer conjugates with significantly enhanced stability, presumably due to the high molecular weight polymer preventing autolysis of the α-chymotrypsin. Graphical abstract: Highlights: Bioconjugates between chymotrypsin and polymers made by RAFT were synthesized. The chymotrypsin–polymer conjugates retained enzymatic activity. High molecular weight polymers enhanced the protein's stability over time.