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Fabrication of high-capacity cation-exchangers for protein adsorption: Comparison of grafting-from and grafting-to approaches
Zhao, Ming1; Liu, Run1; Luo, Jian3; Sun, Yan1,2; Shi, Qinghong1,2,3
刊名FRONTIERS OF CHEMICAL SCIENCE AND ENGINEERING
2019-03-01
卷号13期号:1页码:120-132
关键词polymer-grafted ionic exchanger grafting technique protein adsorption atom transfer radical polymerization -globulin
ISSN号2095-0179
DOI10.1007/s11705-018-1730-y
英文摘要In this work, we have synthesized two polymer-grafted cation exchangers: one via the grafting-from approach, in which sulfopropyl methacrylate (SPM) is grafted through atom transfer radical polymerization onto Sepharose FF (the thus resulting exchanger is referred as Sep-g-SPM), and another via the grafting-to approach, in which the polymer of SPM is directly coupled onto Sepharose FF (the thus resulting exchanger is called as Sep-pSPM). Protein adsorption on these two cation exchangers have been also investigated. At the same ligand density, Sep-g-SPM has a larger accessible pore radius and a smaller depth of polymer layer than SeppSPM, due to the controllable introduction of polymer chains with the regular distribution of the ligand. Therefore, high-capacity adsorption of lysozyme and -globulin could be achieved simultaneously in Sep-g-SPM with an ionic capacity (IC) of 308 mmol$L-1. However, Sep-pSPM has an irregular chain distribution and different architecture of polymer layer, which lead to more serious repulsive interaction to proteins, and thus Sep-pSPM has a lower adsorption capacity for -globulin than Sep-g-SPM with the similar IC. Moreover, the results from protein uptake experiments indicate that the facilitated transport of adsorbed -globulin occurs only in Sep-pSPM and depends on the architecture of polymer layers. Our research provides a clear clue for the development of high-performance protein chromatography.
资助项目National Natural Science Foundation of China[21476166] ; National Natural Science Foundation of China[21236005] ; Open Funding Project of the State Key Laboratory of Biochemical Engineering[2014KF-03] ; Tianjin Natural Science Foundation[15JCYBJC48500]
WOS关键词ION-EXCHANGE ; BINDING ORIENTATION ; TRANSPORT ; CHROMATOGRAPHY ; ADSORBENTS ; LYSOZYME ; KINETICS ; AGAROSE ; MEDIA ; SIZE
WOS研究方向Engineering
语种英语
出版者SPRINGER
WOS记录号WOS:000460491000011
资助机构National Natural Science Foundation of China ; Open Funding Project of the State Key Laboratory of Biochemical Engineering ; Tianjin Natural Science Foundation
内容类型期刊论文
源URL[http://ir.ipe.ac.cn/handle/122111/28325]  
专题中国科学院过程工程研究所
通讯作者Shi, Qinghong
作者单位1.Tianjin Univ, Dept Biochem Engn, Sch Chem Engn & Technol, Tianjin 300350, Peoples R China
2.Tianjin Univ, Key Lab Syst Bioengn, Minist Educ, Tianjin 300072, Peoples R China
3.Chinese Acad Sci, State Key Lab Biochem Engn, Inst Proc Engn, Beijing 100190, Peoples R China
推荐引用方式
GB/T 7714
Zhao, Ming,Liu, Run,Luo, Jian,et al. Fabrication of high-capacity cation-exchangers for protein adsorption: Comparison of grafting-from and grafting-to approaches[J]. FRONTIERS OF CHEMICAL SCIENCE AND ENGINEERING,2019,13(1):120-132.
APA Zhao, Ming,Liu, Run,Luo, Jian,Sun, Yan,&Shi, Qinghong.(2019).Fabrication of high-capacity cation-exchangers for protein adsorption: Comparison of grafting-from and grafting-to approaches.FRONTIERS OF CHEMICAL SCIENCE AND ENGINEERING,13(1),120-132.
MLA Zhao, Ming,et al."Fabrication of high-capacity cation-exchangers for protein adsorption: Comparison of grafting-from and grafting-to approaches".FRONTIERS OF CHEMICAL SCIENCE AND ENGINEERING 13.1(2019):120-132.
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