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Published on: April 22, 2016
A chaperonin as protein nanoreactor for atom-transfer radical polymerization
Kasper Renggli1, Martin G Nussbaumer, Raphael Urbani
1Department of Chemistry, University of Basel, Klingelbergstrasse 80, 4056 Basel (Switzerland).
The archaeal group II chaperonin thermosome (THS) functions as a nanoreactor for atom-transfer radical polymerization (ATRP). This protein cage confines polymerization, yielding narrowly dispersed polymers with low polydispersity indices (PDIs).
Area of Science:
- Biochemistry
- Polymer Chemistry
- Nanotechnology
Background:
- Group II chaperonins, like thermosome (THS) from Thermoplasma acidophilum, are protein complexes involved in protein folding.
- Atom-transfer radical polymerization (ATRP) is a controlled polymerization technique.
Purpose of the Study:
- To investigate the potential of the archaeal group II chaperonin thermosome (THS) as a nanoreactor for controlled polymerization.
- To evaluate the influence of the THS nanoreactor on the atom-transfer radical polymerization (ATRP) of specific monomers.
Main Methods:
- Entrapment of a copper catalyst within the THS protein cage.
- Confining ATRP of N-isopropyl acrylamide and poly(ethylene glycol)methylether acrylate within the THS nanoreactor.
- Comparison with control reactions using a globular protein-catalyst conjugate.
Main Results:
- The THS nanoreactor successfully confined ATRP, allowing polymer release through its pores.
- Narrowly dispersed polymers with polydispersity indices (PDIs) as low as 1.06 were achieved.
- Control reactions yielded polymers with PDIs above 1.84, indicating less control.
Conclusions:
- The archaeal thermosome (THS) serves as an effective protein-based nanoreactor for controlled atom-transfer radical polymerization (ATRP).
- Utilizing THS as a nanoreactor significantly improves polymer dispersity compared to conventional protein-catalyst conjugates.
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