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首页> 外文期刊>RSC Advances >Dicarboxyl-terminated iron(ii) clathrochelates as ICD-reporters for globular proteins
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Dicarboxyl-terminated iron(ii) clathrochelates as ICD-reporters for globular proteins

机译：二羧基封端的铁（II）Clathrochelates作为球状蛋白的ICD-记者

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Cage metal complexes iron( II ) clathrochelates, which are inherently CD silent, were discovered to demonstrate intensive output in induced circular dichroism (ICD) spectra upon their assembly to albumins. With the aim to design clathrochelates as protein-sensitive CD reporters, the approach for the functionalization of one chelate α-dioximate fragment of the clathrochelate framework with two non-equivalent substituents was developed, and constitutional isomers of clathrochelate with two non-equivalent carboxyphenylsulfide groups were synthesized. The interaction of designed iron( II ) clathrochelates and their symmetric homologues with globular proteins (serum albumins, lysozyme, β-lactoglobulin (BLG), trypsin, insulin) was studied by protein fluorescence quenching and CD techniques. A highly-intensive ICD output of the clathrochelates was observed upon their association with albumins and BLG. It was shown that in the presence of BLG, different clathrochelate isomers gave spectra of inverted signs, indicating the stabilization of opposite configurations ( Λ or Δ ) of the clathrochelate framework in the assembly with this protein. So, we suggest that the isomerism of the terminal carboxy group determined preferable configurations of the clathrochelate framework for the fixation in the protein binding site. MALDI TOF results show the formation of BLG–clathrochelate complex with ratio 1?:?1. Based on the docking simulations, the binding of the clathrochelate molecule (all isomers) to the main BLG binding site (calyx) in its open conformation is suggested. The above results point that the variation of the ribbed substituents at the clathrochelate framework is an effective tool to achieve the specificity of clathrochelate ICD reporting properties to the target protein.
机译：笼式金属络合物铁（ii）旋转沉默的铁鼠（II）Clathrochelates，被发现在其组装中展示诱导圆形二色性（ICD）光谱到白藜芦醇蛋白的密集输出。随着将Clathrochelates设计为蛋白质敏感CD记者的方法，开发了一种具有两个非等同取代基的Clathrochelate框架的螯合α-术骨架的官能化的方法，以及具有两个非等效羧基硫醚基团的Clathrochelate的构成异构体被合成了。通过蛋白荧光猝灭和CD技术研究了设计的铁（II）Clathrochelates及其对称同源物与球状蛋白的对称同源物（血清酶，溶菌酶，β-乳糖蛋白（BLG），胰蛋白酶，胰岛素）。在与蛋白质和BLG的关联时观察到Clathrochelates的高度密集的ICD输出。结果表明，在BLG存在下，不同的Clathrochelate异构体具有倒置符号的光谱，表明用该蛋白质在组件中的Clathrochelate框架的相反构型（λ或δ）的稳定性。因此，我们建议终端羧基的异构性确定蛋白质结合位点中的固定的Clathrochelate框架的优选配置。 MALDI TOF结果显示BLG-Clathrochelate复合物的形成1？：？1。基于对接模拟，提出了Clatrochelate分子（所有异构体）在其开放构象中与主BLG结合位点（Calyx）的结合。上述结果点认为肋骨晶体框架上的肋取代基的变化是实现Clathrochelate ICD报告性能与靶蛋白的特异性的有效工具。

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