A Chaperonin as Protein Nanoreactor for Atom-Transfer Radical Polymerization

被引：40

作者：

Renggli, Kasper ^{[2
]}

Nussbaumer, Martin G. ^{[2
]}

Urbani, Raphael ^{[2
]}

Pfohl, Thomas ^{[2
]}

Bruns, Nico ^{[1
,2
]}

机构：

[1] Univ Fribourg, Adolphe Merkle Inst, CH-1723 Marly, Switzerland

[2] Univ Basel, Dept Chem, CH-4056 Basel, Switzerland

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2014年 / 53卷 / 05期

基金：

瑞士国家科学基金会;

关键词：

chaperone proteins; controlled/living radical polymerization; nanoreactor; polymerization; thermosome; GROUP-II CHAPERONIN; FUTURE PERSPECTIVES; BLOCK-COPOLYMERS; ATRP; THERMOSOME; DESIGN; P22; ENCAPSULATION; ORGANELLES; MECHANISM;

D O I：

10.1002/anie.201306798

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：1443 / 1447

页数：5

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