Physico-Chemical nanomaterials science

Supramolecular binding of the designed meta- and para-carboxyl-terminated monoribbed-difunctionalized iron(II) clathrochelate isomers to a transport albumin’s macromolecule

Chornenka N.V.1, Vakarov S.V.1, Kovalska V.B.2, Gumienna-Kontecka E.3, Voloshin Y.4

1 V.I. Vernadsky Institute of General and Inorganic Chemistry NASU, Kyiv.
e-mail:nina.v.chornenka@gmail.com
2 Institute of Molecular Biology and Genetics, NASU, Kyiv.
3 Faculty of Chemistry, University of Wroclaw, Wroclaw, Poland.
4 A.N. Nesmeyanov Institute of Organoelement Compounds RAS, Moscow, Russia.

Fig.1. ICD spectra of the HSA – clathrochelate (1 or 2) assemblies. 	
Changes in the shapes and in the intensities of the clathrochelate-based induced CD (ICD) spectra of clathrochelate – protein assemblies are known to reflect both the conformation transitions of proteins macromolecules and their structural alterations. ICD outputs of two meta- and para-carboxyl-terminated constitutional isomers (1 and 2) of a monomorpholinemono-carboxyphenyl-sulfide iron(II) clathrochelate with two functionalizing biorelevant vic-substituents on their supramolecular assembling with human serum albumin (HSA) were measured. They gave the pronounced clathrochelate-based CD outputs with intensities 17.4 and 11.1 mdeg, respectively, in its presence, possessing the inverted shapes: ICD spectrum of the HSA – clathrochelate 2 assembly contains two negative (350 and 520 nm), and one positive (440 nm) bands, while that for its meta-substituted analog 1 possesses a “classical” possess two maxima and one minimum (Fig.1). So, their constitutional isomerism strongly affected protein-induced clathrochelate-based CD-activity of these designed cage molecules.

The project leading to these results has received Funding from the European Union's Horizon 2020 research and innovation program under the Marie Sklodowska-Qurie grant agreement No 778245.