Decoupled Ion Transport in Protein-Based Solid Electrolyte through Ab Initio Calculations and Experiments
Decoupled Ion Transport in Protein-Based Solid Electrolyte through Ab Initio Calculations and Experiments
复制标题
通过从头计算和实验解耦蛋白质固体电解质中的离子传输
DOI：
10.1021/acs.jpclett.1c02412
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Liu, Jin
中科院分区：
文献类型：
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作者：
Ying, Chunhua;Fu, Xuewei;Zhong, Wei-Hong;Liu, Jin
离子运动的解耦和分段弛豫对于开发高离子导电性和高机械性能的新型固体聚合物电解质具有重要意义。我们以前的工作提出了一种新型的蛋白质基固体电解质中的解耦离子传输。在这里，我们通过第一性原理密度泛函理论(DFT)计算研究了真空空间中离子相互作用/输运的详细机制。具体地说，我们研究了蛋白质中带电氨基酸的重要作用。结果表明，荷电氨基酸(Arg和Lys)对阴离子(ClO4-)有很强的锁定作用。当被锁定在适当的位置(由氨基酸的分子结构确定)时，阴离子可以提供额外的跳跃位置并促进Li+的运输。这一发现得到了我们对两种蛋白质固体电解质的实验的支持，在这两种固体电解质中，大豆蛋白(富含带电氨基酸)的电解质与玉米醇溶蛋白(缺少带电氨基酸)的电解质相比，具有更高的离子电导率和更低的活化能。
Decoupling the ion motion and segmental relaxation is significant for developing advanced solid polymer electrolytes with high ionic conductivity and high mechanical properties. Our previous work proposed a decoupled ion transport in a novel protein-based solid electrolyte. Herein, we investigate the detailed ion interaction/transport mechanisms through first-principles density functional theory (DFT) calculations in a vacuum space. Specifically, we study the important roles of charged amino acids from proteins. Our results show that the charged amino acids (i.e., Arg and Lys) can strongly lock anions (ClO4–). When locked at a proper position (determined from the molecular structure of amino acids), the anions can provide additional hopping sites and facilitate Li+transport. The findings are supported from our experiments of two protein solid electrolytes, in which the soy protein (with plenty of charged amino acids) electrolyte shows much higher ionic conductivity and lower activation energy in comparison to the zein (lack of charged amino acids) electrolyte.