Characterization of cerium (III) ion binding to surface‐immobilized EF‐hand loop I of calmodulin

Characterization of cerium (III) ion binding to surface‐immobilized EF‐hand loop I of calmodulin
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与钙调蛋白表面固定的 EF-手环 I 结合的铈 (III) 离子的表征

DOI:
10.1002/pep2.24133
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发表时间:
2019
期刊:
影响因子:
2.4
通讯作者:
Renner, Julie N.
Renner, Julie N.
中科院分区:
医学4区
文献类型:
--
作者:
Xu, MingYuan;Su, Zihang;Renner, Julie N.

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铈具有广泛的当前和新兴应用,并且铈离子与固体基质的结合对于铈回收或先进材料合成非常重要。在本研究中,我们研究了源自钙调蛋白 EF 手环 I 的表面结合肽对铈 (III) 离子的亲和力,并将结果与​​乱序对照进行比较。通过石英晶体微天平与耗散获得的结果用于估计结合的 EF-hand 环 I 肽和铈 (III) 离子 (1.3±0.1 μM) 之间的解离常数,这与本工作和文献中报告的溶液中 EF-hand 肽和铈离子测量的其他解离常数 (0.95-5.8 μM) 相当。圆二色性还表明该肽与溶液中的铈 (III) 离子结合,并在结合后经历二级结构变化。总的来说,这项研究表明 EF-hand 环肽能够在溶液中以及附着在固体基质上时结合铈 (III) 离子。
Cerium has a wide range of current and emerging applications, and the binding of cerium ions to solid substrates is important for cerium recovery, or in advanced material synthesis. In this study, we investigate the affinity of a surface‐bound peptide derived from the EF‐hand loop I of calmodulin for cerium (III) ions and compare the results to a scrambled control. Results obtained via quartz crystal microbalance with dissipation are used to estimate the dissociation constant between the bound EF‐hand loop I peptide and cerium (III) ions (1.3 ± 0.1 μM), which is comparable with other dissociation constants measured for EF‐hand peptides and cerium ions in solution reported this work and in literature (0.95‐5.8 μM). Circular dichroism also suggests that the peptide binds to cerium (III) ions in solution, and undergoes a secondary structural change upon binding. Overall, this study shows that EF‐hand loop peptides are capable of binding cerium (III) ions in solution and when attached to a solid substrate.
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