共聚物
两亲性
木筏
甲基丙烯酸酯
化学
链式转移
单体
化学工程
低临界溶液温度
组合化学
材料科学
高分子化学
有机化学
自由基聚合
聚合物
工程类
作者
Yongming Zeng,Tianchi Xu,Xiaofang Hou,Jiang Liu,Changqing Liu,Zhaosen Chang,Jing Fang,Dongzhong Chen
出处
期刊:ACS applied polymer materials
[American Chemical Society]
日期:2023-04-18
卷期号:5 (5): 3777-3791
标识
DOI:10.1021/acsapm.3c00390
摘要
To achieve convenient storage of bioactive materials such as protein enzymes (proteases) at ambient temperature, with both their spatial structure and biocatalytic activity well retained, is highly appealing but challenging. Herein, a variety of amphiphilic random copolymers have been well synthesized via reversible addition–fragmentation chain transfer (RAFT) copolymerization of sulfobetaine methacrylate (SBMA) and various length fluoroalkyl methacrylate monomers. By simultaneously introducing fluoroalkyl and zwitterionic segments in random copolymerization, such kinds of amphiphilic random copolymers combined the advantages of both polyzwitterionic and fluoropolymers, which were capable of constructing uniform tiny single-chain nanoparticles (SCNPs) of around 10 nm in a wide range of compositions and fabrication conditions from aqueous solutions. Through intramolecular self-folding of the fluorinated alkyl segments to constitute the compact inner cores and the superhydrophilic zwitterionic SBMA polymer segments forming the outer passivated layer, the thus obtained SCNPs exhibited remarkable enzyme stabilizing capability through morphological adjustment, hydration, and heterocoagulation mechanisms for the investigated glucose oxidase (GOx) and horse radish peroxidase (HRP), acting like artificial molecular chaperones. Moreover, enzyme catalytic activity enhancement in the HRP@SCNPs system was well demonstrated with a representative enzyme-catalyzed cascade oxidization reaction for the synthesis of an azobenzene chromophore. Therefore, this work provides a facile fabricating strategy for SCNPs from well-synthesized amphiphilic random copolymers via RAFT, which may serve as promising stabilizers for ambient temperature storage and activity preservation of proteases.
科研通智能强力驱动
Strongly Powered by AbleSci AI