Well-Defined Macromolecules Using Horseradish Peroxidase as a RAFT Initiase

被引:67
作者
Danielson, Alex P. [1 ]
Bailey-Van Kuren, Dylan [1 ]
Lucius, Melissa E. [1 ]
Makaroff, Katherine [1 ]
Williams, Cameron [1 ]
Page, Richard C. [1 ]
Berberich, Jason A. [2 ]
Konkolewicz, Dominik [1 ]
机构
[1] Miami Univ, Dept Chem & Biochem, 651 E High St, Oxford, OH 45056 USA
[2] Miami Univ, Dept Chem Paper & Biomed Engn, Miami, FL USA
关键词
enzyme catalysis; heme proteins; polymerization; protein modifications; raft polymerization; FREE-RADICAL POLYMERIZATION; ENZYME-MEDIATED INITIATION; ACRYLAMIDE POLYMERIZATION; METHYL-METHACRYLATE; CHAIN TRANSFER; GRAFTING-FROM; PROTEIN; TEMPERATURE; POLYMERS;
D O I
10.1002/marc.201500633
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
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.
引用
收藏
页码:362 / 367
页数:6
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