Induced CD of iron(ii ) clathrochelates: sensing of the structural and conformational alterations of serum albumins
| Autor: | Marina V. Kuperman, Sergiy M. Yarmoluk, Vladyslava B. Kovalska, Yan Z. Voloshin, Oleg A. Varzatskii, Serhii V. Vakarov, Slawomir Potocki, Mykhaylo Yu. Losytskyy, Elzbieta Gumienna-Kontecka |
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| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Molecular Conformation Biophysics Serum albumin Biochemistry Biomaterials Metal 03 medical and health sciences Coordination Complexes Structural isomer Animals Humans Molecule Ferrous Compounds Bovine serum albumin Serum Albumin Molecular Structure 030102 biochemistry & molecular biology biology Chemistry Circular Dichroism Visible spectral range Metals and Alloys Serum Albumin Bovine Isothermal titration calorimetry Protein tertiary structure Crystallography 030104 developmental biology Chemistry (miscellaneous) visual_art visual_art.visual_art_medium biology.protein Cattle |
| Zdroj: | Metallomics |
| ISSN: | 1756-591X 1756-5901 |
| DOI: | 10.1039/c8mt00278a |
| Popis: | An ability of inherently achiral macrobicyclic metal complexes iron(II) clathrochelates to acquire an induced CD (ICD) output in the visible spectral range upon interaction with bovine serum albumin (BSA) was recently discovered. In the present work, the CD-reporting properties of iron(II) clathrochelates to proteins and the thermodynamic parameters of their binding to albumins are evaluated. It is shown that iron(II) clathrochelates functionalized by six ribbed carboxyphenylsulfide groups are able to discriminate between serum albumins of relative structure (here human and bovine albumins) by giving distinct ICD spectra. Besides, by the variation of the shape and intensity of CD bands, these cage metal complexes reflect the pH-triggered alterations of the tertiary structure of albumins. The constitutional isomerism (ortho-, meta- or para-isomers) of terminal carboxyphenylsulfide groups of iron(II) clathrochelates strongly affects both the character of their ICD output upon binding with proteins and the parameters of the formed guest–host associates. Using isothermal titration calorimetry, it was determined that cage metal complexes bearing meta- and ortho-isomers of carboxyphenylsulfide groups possess higher association constants (Ka B 2 104 M1 ) and clathrochelate-to-BSA binding ratios (n = 2) than the para-isomer (Ka B 5 103 M1 , n = 1). The iron(II) clathrochelates are suggested to be potential molecular three-dimensional scaffolds for the design of CD-sensitive reporters able to recognize specific elements of protein surfaces. |
| Databáze: | OpenAIRE |
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