详细信息

Protein-Polyelectrolyte Interaction: Thermodynamic Analysis Based on the Titration Method  ( SCI-EXPANDED收录 EI收录)  

文献类型:期刊文献

英文题名:Protein-Polyelectrolyte Interaction: Thermodynamic Analysis Based on the Titration Method

作者:Wang, Xiaohan[1];Zheng, Kai[1];Si, Yi[2];Guo, Xuhong[1,3,4];Xu, Yisheng[1,3,4]

机构:[1]East China Univ Sci & Technol, State Key Lab Chem Engn, Shanghai 200237, Peoples R China;[2]Fudan Univ, Inst Vasc Surg, 180 Fenglin Rd, Shanghai 200032, Peoples R China;[3]East China Univ Sci & Technol, Int Joint Res Ctr Green Energy Chem Engn, Shanghai 200237, Peoples R China;[4]Shihezi Univ, Engn Res Ctr Xinjiang Bingtuan Mat Chem Engn, Xinjiang 832000, Peoples R China

年份:2019

卷号:11

期号:1

外文期刊名:POLYMERS

收录:;EI(收录号:20190206361618);WOS:【SCI-EXPANDED(收录号:WOS:000457202000082)】;

基金:This research was funded by the National Science Foundation of China (NSFC; No. 21676089, 81470581). This work was also sponsored by Shanghai Talent Development Fund (2017038), Interantional One belt One Road Collaboration Project of Shanghai (18490740300), the Fundamental Research Funds for the Central Universities (222201717013, 22221818014), and 111 Project Grant (B08021).

语种:英文

外文关键词:polyelectrolyte; complexation; electrostatics; thermodynamic analysis; isothermal titration calorimetry

摘要:This review discussed the mechanisms including theories and binding stages concerning the protein-polyelectrolyte (PE) interaction, as well as the applications for both complexation and coacervation states of protein-PE pairs. In particular, this review focused on the applications of titration techniques, that is, turbidimetric titration and isothermal titration calorimetry (ITC), in understanding the protein-PE binding process. To be specific, by providing thermodynamic information such as pH(c), pH(phi), binding constant, entropy, and enthalpy change, titration techniques could shed light on the binding affinity, binding stoichiometry, and driving force of the protein-PE interaction, which significantly guide the applications by utilization of these interactions. Recent reports concerning interactions between proteins and different types of polyelectrolytes, that is, linear polyelectrolytes and polyelectrolyte modified nanoparticles, are summarized with their binding differences systematically discussed and compared based on the two major titration techniques. We believe this short review could provide valuable insight in the understanding of the structure-property relationship and the design of applied biomedical PE-based systems with optimal performance.

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