A Chaperonin as Protein Nanoreactor for Atom-Transfer Radical Polymerization
Angew. Chem. Int. Ed. 2014, 53, 1443-1447, 10.1002/anie.201306798
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.
Metal: CuLigand type: N,N,N’,N’-tetraethyldiethylene triamine (TEDETA)Host protein: Thermosome (THS)Anchoring strategy: CovalentOptimization: ---Reaction: PolymerizationMax TON: ---ee: ---PDB: ---Notes: Non-ROMP