Abstract—

CD testing of a supramolecular binding of three constitutional isomers (ortho-, meta-, and para-substituted) of an inherently CD-silent monomethinemonocarboxyphenylsulfide iron(II) clathrochelate to globular proteins (serum albumins BSA and HSA, lysozyme and β-lactoglobulin) was performed. This type of isomerism is found to strongly affect an induced CD-activity of these clathrochelates upon their binding to protein. To study an effect of the additional ribbed functionalization on protein’s sensing properties, the CD outputs of clathrochelate analogs with biorelevant morpholine group were studied. Such a functionalization is found to substantially affect the protein’s CD-sensing properties; this is explained by a formation of hydrogen bonds between this substituent and aminoacid residues of a protein binding site, thus affecting and altering an arrangement of the corresponding clathrochelate–protein assembly. Molecular docking calculations were performed for structural modeling of the BSA–clathrochelate assemblies and to estimate an energy of these supramolecular processes.

中文翻译：

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单羧基苯基硫化铁（II）笼形螯合物作为光学报道分子，利用诱导的圆二色光谱感测蛋白质的结构。

摘要-

CD测试三种超构分子（邻位，间位和对位）的超分子结合将固有的CD沉默的单次甲基单羧基苯基硫醚铁（II）笼形螯合物取代成球形蛋白质（血清白蛋白BSA和HSA，溶菌酶和β-乳球蛋白）。发现这种类型的异构现象在它们与蛋白质结合时强烈影响这些笼形螯合物的诱导的CD-活性。为了研究额外的带肋功能化对蛋白质感测特性的影响，研究了具有生物相关性吗啉基团的笼形螯合物类似物的CD输出。发现这种功能化实质上影响了蛋白质的CD敏感特性。这可以通过该取代基与蛋白质结合位点的氨基酸残基之间形成氢键来解释，从而影响并改变了笼形螯合物-蛋白质组装体的排列方式。