Preparation, Characterization And Study Of Biological Potency In Binuclear Zinc(II) Complex Of Dithiocarbamate Derivatives
عنوان مقاله: Preparation, Characterization And Study Of Biological Potency In Binuclear Zinc(II) Complex Of Dithiocarbamate Derivatives
شناسه ملی مقاله: IICC20_126
منتشر شده در بیستمین سمینار شیمی معدنی ایران در سال 1397
شناسه ملی مقاله: IICC20_126
منتشر شده در بیستمین سمینار شیمی معدنی ایران در سال 1397
مشخصات نویسندگان مقاله:
somaye Shahrakia - Department of Chemistry, University of Zabol, Zabol, Iran
Fereshteh Shiri, - Department of Chemistry, University of Zabol, Zabol, Iran
Hossein forouzandeh-moghadam - Department of Chemistry, University of Zabol, Zabol, Iran
خلاصه مقاله:
somaye Shahrakia - Department of Chemistry, University of Zabol, Zabol, Iran
Fereshteh Shiri, - Department of Chemistry, University of Zabol, Zabol, Iran
Hossein forouzandeh-moghadam - Department of Chemistry, University of Zabol, Zabol, Iran
It is, essential to investigate the interactions between drugs and carrier proteins in order to specify the pharmacology and pharmacodynamics of drugs (1). A binuclear dithiocarbamate Zn(II) complex [(phen)Zn(μ-pr-dtc)Zn(phen)](NO3)2 (where phen = 1,10-phenanthroline, pr-dtc = propylenebisdithiocarbamate, Fig. 1) was synthesized and characterized in the present study. The formulated complex was evaluated for in vitro antioxidant activity as radical scavengers against 1,1-diphenyl-2-picrylhydrazyl radicals (DPPH.). According to the results, antioxidant activity of Zn complex (IC50 = 21 mg L-1) was effective. Biophysical techniques along with computational modeling were employed to examine the binding of this complex with bovine β-lactoglobulin (βLG) as the model protein. The trial findings revealed an interaction between binuclear complex and βLG with a modest binding affinity (Kb = 6.01 × 104 M−1. An intense fluorescence quenching of protein through a static quenching mechanism was occurred due to the binding of complex to βLG. Hydrogen bonds and Van der Waals forces was the main stabilizing forces in the development of drug-protein complex. Analysis of protein-ligand docking demonstrated binding of complex to residues placed in the site B of βLG
کلمات کلیدی: Carrier protein; Antioxidant agent; Molecular docking
صفحه اختصاصی مقاله و دریافت فایل کامل: https://civilica.com/doc/876427/