A chaperonin as protein nanoreactor for atom-transfer radical polymerization

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

doi:10.1002/anie.201306798

A chaperonin as protein nanoreactor for atom-transfer radical polymerization

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

Pure And Applied Chemistry

Research output: Contribution to journal › Article

25 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	1443-1447
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	53
Issue number	5
DOIs	https://doi.org/10.1002/anie.201306798
Publication status	Published - 27 Jan 2014

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Keywords

chaperone proteins
controlled/living radical polymerization
nanoreactor
polymerization
thermosome

Cite this

Renggli, K., Nussbaumer, M. G., Urbani, R., Pfohl, T., & Bruns, N. (2014). A chaperonin as protein nanoreactor for atom-transfer radical polymerization. Angewandte Chemie - International Edition, 53(5), 1443-1447. https://doi.org/10.1002/anie.201306798

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10.1002/anie.201306798

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