A chaperonin as protein nanoreactor for atom-transfer radical polymerization

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

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)


The group II chaperonin thermosome (THS) from the archaea Thermoplasma acidophilum is reported as nanoreactor for atom-transfer radical polymerization (ATRP). A copper catalyst was entrapped into the THS to confine the polymerization into this protein cage. THS possesses pores that are wide enough to release polymers into solution. The nanoreactor favorably influenced the polymerization of Nisopropyl acrylamide and poly(ethylene glycol)methylether acrylate. Narrowly dispersed polymers with polydispersity indices (PDIs) down to 1.06 were obtained in the protein nanoreactor, while control reactions with a globular protein- catalyst conjugate only yielded polymers with PDIs above 1.84.

Original languageEnglish
Pages (from-to)1443-1447
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number5
Publication statusPublished - 27 Jan 2014


  • chaperone proteins
  • controlled/living radical polymerization
  • nanoreactor
  • polymerization
  • thermosome


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