Multispectroscopic and molecular modeling approach to investigate the interaction of zinc(II) complex containing amino alcohol ligand with biomacromolecule HSA

Document Type : Original Article

Authors

1 Department of Inorganic Chemistry, Faculty of Chemistry, Razi University, Kermanshah, IRAN

2 Inorganic chem. dept. Chem. Faculty, Razi University, Kermanshah, IRAN

3 Department of Inorganic Chemistry, Faculty of Chemistry, Urmia University, Urmia, Iran

10.22126/bmcj.2023.2624

Abstract

In this study, a zinc(II) complex containing amino alcohol ligand; [(cis-2-((2-((2-hydroxyethyl)aminoethylamino)benzene-1-ol) dibromo zinc(II)] or briefly [Zn(HAIP)Br2]) has been synthesized and the interaction with Human Serum Albumin (HSA) studied using various spectroscopic techniques and molecular docking. The UV–vis absorption spectra of HSA decreased by adding the complex and therefore, suggesting that this complex led to a change in conformation of α-helical of protein. The fluorescence results showed that the HSA emission was quenched by zinc(II) complex through static quenching. In addition, the presence of hydrogen bond and van der Waals force was confirmed due to thermodynamic parameters. The molecular docking was used to simulate and predict the binding site of zinc(II) complex to albumin and to authenticate experimental results. There is a good agreement between the free binding energy of docking simulation and the binding constant of fluorescence experiments. These results very clearly authenticate that zinc complex–HSA docked model is in approximate correlation with our experimental results.

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