Journal article
A chaperonin as protein nanoreactor for atom-transfer radical polymerization.
- Renggli K Department of Chemistry, University of Basel, Klingelbergstrasse 80, 4056 Basel (Switzerland).
- Nussbaumer MG
- Urbani R
- Pfohl T
- Bruns N
- 2014-01-25
Published in:
- Angewandte Chemie (International ed. in English). - 2014
chaperone proteins
controlled/living radical polymerization
nanoreactor
polymerization
thermosome
Acrylamides
Catalysis
Chaperonins
Copper
Free Radicals
Ligands
Nanotechnology
Polyamines
Polymerization
Thermoplasma
Thermosomes
English
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 N-isopropyl 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.
- Language
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- English
- Open access status
- closed
- Identifiers
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- DOI 10.1002/anie.201306798
- PMID 24459061
- Persistent URL
- https://sonar.ch/global/documents/273027
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