Well‐Defined Macromolecules Using Horseradish Peroxidase as a RAFT Initiase. Issue 4 (8th January 2016)

• Record Type: Journal Article
• Authors: Danielson, Alex P.; Van Kuren, Dylan Bailey‐; Lucius, Melissa E.; Makaroff, Katherine; Williams, Cameron; Page, Richard C.; Berberich, Jason A.; Konkolewicz, Dominik
• Is Part Of: Macromolecular rapid communications. Volume 37:Issue 4(2016)
• Page Start: 362
• Page End: 367
• Publication Date: 2016-01-08
• Subjects: enzyme catalysis -- heme proteins -- polymerization -- protein modifications -- raft polymerization; Macromolecules -- Periodicals; Polymers -- Periodicals; Chemistry -- Periodicals; 547.705
• DOI: 10.1002/marc.201500633
• Languages: English
• ISSNs: 1022-1336

Abstract

Abstract : Enzymatic catalysis and control over macromolecular architectures from reversible addition‐fragmentation chain transfer polymerization (RAFT) are combined to give a new method of making polymers. Horseradish peroxidase (HRP) is used to catalytically generate radicals using hydrogen peroxide and acetylacetone as a mediator. RAFT is used to control the polymer structure. HRP catalyzed RAFT polymerization gives acrylate and acrylamide polymers with relatively narrow molecular weight distributions. The polymerization is rapid, typically exceeding 90% monomer conversion in 30 min. Complex macromolecular architectures including a block copolymer and a protein‐polymer conjugate are synthesized using HRP to catalytically initiate RAFT polymerization. Abstract : RAFT polymerization is performed using horseradish peroxidase to catalytically generate radicals. Well‐defined homo, block polymers are synthesized as well as a protein‐polymer conjugate