Biocatalytic atom transfer radical polymerization in a protein cage nanoreactor

Kasper Renggli, Nora Sauter, Martin Rother, Martin G. Nussbaumer, Raphael Urbani, Thomas Pfohl, Nico Bruns

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)
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Incorporation of the ATRP-catalyzing enzyme horseradish peroxidase (HRP) into the cavities of the group II chaperonin thermosome is demonstrated. The resulting nanoreactor was used to polymerize an acrylate under ARGET ATRP conditions. The confined space within the protein cage results in poly(ethylene glycol) methyl ether acrylate (PEGA) with lower molecular weights (poly(styrene)-apparent Mn = 4400 g mol-1) as well as narrower molecular weight distributions (Đ = 1.08) compared to polymerizations with the free ATRPase (Mn = 43700 g mol-1 and a Đ of 1.23).

Original languageEnglish
Pages (from-to)2133-2136
Number of pages4
JournalPolymer Chemistry
Issue number14
Early online date13 Mar 2017
Publication statusPublished - 14 Apr 2017


  • horseradish peroxidase
  • protein cages
  • polymerization


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