Preparation, characterization and comparison of biological potency in two new Zn(II) and Pd(II) complexes of butanedione monoxime derivatives
| Autor: | Abolfazl Fathollahi Zonouz, Somaye Shahraki, Alireza Oveisi Keikha, Hojat Samareh Delarami, Zahra Azizi, Ali Heydari |
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| Rok vydání: | 2020 |
| Předmět: |
Metal ions in aqueous solution
Diacetyl Molecular Dynamics Simulation Ligands Medicinal chemistry chemistry.chemical_compound Structure-Activity Relationship Structural Biology Potency Molecular Biology Density Functional Theory Schiff Bases Schiff base Binding Sites Molecular Structure Ligand Spectrum Analysis General Medicine Free Radical Scavengers Models Theoretical Molecular Docking Simulation Zinc chemistry Lead Carrier protein Thermodynamics Density functional theory Carrier Proteins Butanedione monoxime Protein Binding |
| DOI: | 10.6084/m9.figshare.7938311.v2 |
| Popis: | A novel Schiff base ligand (2-iminothiophenol-2,3-butanedione monoxime, ITBM) and its complexes with Pd(II) and Zn(II) metal ions ([M(ITBM)2]Cl2) were synthesized and characterized in the present study. The formulated complexes were evaluated for in vitro antioxidant activity as radical scavengers against 1,1-diphenyl-2-picrylhydrazyl radicals (DPPH•). According to the results, antioxidant activity of Pd complex (IC50=36 mg L−1) was more effective than that of Zn(II) complex (IC50=72 mg L−1). Biophysical techniques along with computational modeling were employed to examine the binding of these complexes with human serum albumin (HSA) as the model protein. The trial findings revealed an interaction between Schiff base complexes and HSA with a modest binding affinity [Kb=6.31(±0.11)×104 M−1 for Zn(II) complex and 0.71(±0.05)×104 M−1 for Pd(II) complex at 310 K]. An intense fluorescence quenching of protein through a static quenching mechanism was occurred due to the binding of both complexes to HSA. Hydrogen bonds and van der Waals forces in both examined systems were the main stabilizing forces in the development of drug–protein complex. Based on far-UV-CD observations, the content of α-helical structure in the protein was reduced through induction by both complexes. Analysis of protein–ligand docking demonstrated binding of the two Schiff base complexes to residues placed in the IIA subdomain of HSA. In addition, Zn complex with HSA showed a stronger binding ability than that of Pd complex. Communicated by Ramaswamy H. Sarma |
| Databáze: | OpenAIRE |
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