Dicarboxyl-terminated iron(ii) clathrochelates as ICD-reporters for globular proteins
Kovalska VB, Vakarov S, Losytskyy M, Kuperman M, Chornenka N, Toporivska Y, Gumienna-Kontecka E, Voloshin Y, Varzatskii O, Mokhir A (2019)
Publication Type: Journal article
Publication year: 2019
Journal
Book Volume: 9
Pages Range: 24218-24230
Journal Issue: 42
DOI: 10.1039/c9ra04102h
Abstract
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.
Authors with CRIS profile
Involved external institutions
Princeton BioMolecular Research, Inc.
United States (USA) (US)
National Academy of Sciences of Ukraine (NAN) / Національна академія наук України
Ukraine (UA)
University of Wroclaw / Uniwersytet Wrocławski
Poland (PL)
A.N.Nesmeyanov Institute of Organoelement Compounds (INEOS RAS) / Институт элементоорганических соединений Российской Академии Наук им. А.Н. Несмеянова (ИНЭОС РАН)
Russian Federation (RU)
Vernadsky Institute of general and inorganic chemistry / Інститут загальної та неорганічної хімії імені В. I. Вернадського НАН України
Ukraine (UA)
United States (USA) (US)
National Academy of Sciences of Ukraine (NAN) / Національна академія наук України
Ukraine (UA)
University of Wroclaw / Uniwersytet Wrocławski
Poland (PL)
A.N.Nesmeyanov Institute of Organoelement Compounds (INEOS RAS) / Институт элементоорганических соединений Российской Академии Наук им. А.Н. Несмеянова (ИНЭОС РАН)
Russian Federation (RU)
Vernadsky Institute of general and inorganic chemistry / Інститут загальної та неорганічної хімії імені В. I. Вернадського НАН України
Ukraine (UA)
How to cite
APA:
Kovalska, V.B., Vakarov, S., Losytskyy, M., Kuperman, M., Chornenka, N., Toporivska, Y.,... Mokhir, A. (2019). Dicarboxyl-terminated iron(ii) clathrochelates as ICD-reporters for globular proteins. RSC Advances, 9(42), 24218-24230. https://dx.doi.org/10.1039/c9ra04102h
MLA:
Kovalska, Vladyslava B., et al. "Dicarboxyl-terminated iron(ii) clathrochelates as ICD-reporters for globular proteins." RSC Advances 9.42 (2019): 24218-24230.
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