Study of interaction between the anti-tumor complex of zinc(II) containing Schiff base ligand with human and bovine serum albumin

Subject Areas :

somaye shahraki ¹ (Department of Chemistry, Faculty of Science, University of Zabol, Zabol, Iran)
fatemeh khosravi ² (Department of Chemistry, Faculty of Science, University of Zabol, Zabol, Iran)

Received: 2021-12-12 Accepted : 2022-04-26 Published : 2022-08-23

Keywords: structural changes, Binding/thermodynamic parameters, Human/Bovine serum albumin, Protein interactions, Schiff base complexes,

Abstract :

Due to the growing interest of researchers in the synthesis of new chemical compounds that have diverse medicinal properties, in this study, the interaction of the complex of [Zn(SBL)2]Cl2 (SBL = Schiff base ligand 2(-iminoethyl)piperazine diacetyl monoxime) with human and bovine serum albumin proteins (HSA and BSA) in tris-buffer medium was investigated by spectroscopic methods. The results for both complexes were almost identical, as fluorescence spectroscopy showed that the inherent fluorescence quenching of both proteins is due to the interaction of the zinc complex through a static quenching mechanism. The zinc complex interacted with both proteins with almost the same affinity. Thermodynamic parameters showed the contribution of hydrogen bonding and van der Waals interactions, but the role of hydrophobic interactions is not insignificant due to the presence of the imine group in the complex structure and the small amount of ∆S. Structural changes during the interaction of zinc complex with two proteins were investigated by synchronous‎ fluorescence methods as well as circular dichroism. The results of synchronous‎ ‎ fluorescence showed that during the interaction of the complex with proteins no noticeable polarity change occurred around the tryptophan residue while around the tyrosine residue the polarity changed. The study of circular dichroism spectroscopy also shows a decrease in the content of the alpha helix in both complexes. The results of this study confirm that the interaction of the zinc complex in both proteins is almost similar, so sometimes in pharmacological studies it can be used instead of human protein from its animal family.

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