ATRPases: using nature's catalysts in atom transfer radical polymerizations

Gergely Kali, Tilana B. Silva, Severin J. Sigg, Farzad Seidi, Kasper Renggli, Nico Bruns

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

9 Citations (Scopus)

Abstract

Enzymes are environmentally friendly, non-toxic catalysts that have found many applications in synthetic polymer chemistry. However, until very recently no examples of enzyme-catalyzed, controlled radical polymerizations were known. Here we review the nascent field of biocatalytic atom transfer radical polymerization (ATRP). The heme proteins horseradish peroxidase, hemoglobin and catalase, as well as the copper-containing enzyme laccase have been reported to display catalytic activity in activators regenerated by electron transfer (ARGET) ATRP of two model monomers, N-isopropylacrylamide and poly(ethylene glycol) methyl ether acrylate. Bromine-terminated polymers, low polydispersity indices, linear increase in molecular weight with conversion as well as first-order kinetics indicate ATRP-type mechanisms. However, the first examples of biocatalytic ATRP also show that enzymes are much more complex catalysts than conventional ones.

Original languageEnglish
Title of host publicationProgress in Controlled Radical Polymerization
Subtitle of host publicationMechanisms and Techniques
PublisherAmerican Chemical Society
Pages171-181
Number of pages11
ISBN (Print)9780841226999
DOIs
Publication statusPublished - 1 Jan 2012

Publication series

NameACS Symposium Series
Volume1100
ISSN (Print)0097-6156
ISSN (Electronic)1947-5918

Keywords

  • enzymatic polymerization
  • acrylic monomers
  • enzymes
  • free radical polymerization
  • polydispersity
  • polyethylene glycols
  • polymers
  • atom transfer radical polymerization

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