Hydrophobic core formation and secondary structure elements in uranyl(VI)-binding peptides
Hydrophobic core formation and secondary structure elements in uranyl(VI)-binding peptides
复制标题
铀酰 (VI) 结合肽中的疏水核心形成和二级结构元件
DOI：
10.1039/d1cp05401e
复制
发表时间：
2022
影响因子：
3.3
通讯作者：
Koichiro Takao
中科院分区：
文献类型：
--
作者：
Satoru Tsushima;Koichiro Takao
环肽以及钙调蛋白的修饰EF-手基序已被新设计成实现对铀酰（VI）的高亲和力。环肽可以被改造成在酸性条件下将铀酰（VI）结合到其骨架上，这可以增强其选择性。对于钙调蛋白的修饰EF-手基序，铀酰（VI）和带负电荷的侧链之间的强静电相互作用在实现高亲和力方面发挥着重要作用;然而，在肽的金属结合状态下具有二级结构元件和形成疏水核心也是必不可少的。
Cyclic peptides as well as a modified EF-hand motif of calmodulin have been newly designed to achieve high affinity towards uranyl(VI). Cyclic peptides may be engineered to bind uranyl(VI) to its backbone under acidic conditions, which may enhance its selectivity. For the modified EF-hand motif of calmodulin, strong electrostatic interactions between uranyl(VI) and negatively charged side chains play an important role in achieving high affinity; however, it is also essential to have a secondary structure element and formation of hydrophobic cores in the metal-bound state of the peptide.