Department of Chemistry, University of Zabol, Zabol, Iran.
Department of Chemistry, University of Sistan and Baluchestan, Zahedan, Iran.
Colloids Surf B Biointerfaces. 2017 Dec 1;160:564-571. doi: 10.1016/j.colsurfb.2017.10.026. Epub 2017 Oct 8.
A novel Schiff base Zn(II) complex using a tetradentate Schiff base ligand was synthesized and characterized. The results of cytotoxicity assay revealed that the prepared complex induced cytotoxicity in a breast cancer cell line. Thus, the binding of the Zn(II) complex to human serum albumin (HSA) was investigated using spectroscopic and molecular docking methods. The fluorescence data showed that the Zn(II) complex quenched protein fluorescence by a static quenching mechanism. The binding constant (K), number of binding sites (n), and thermodynamic parameters were calculated and showed that the Zn(II) complex binds to HSA through hydrogen bond and Vander Waals interactions with one binding site. Protein-ligand docking analysis confirmed that the Zn(II) complex binds to residues located in the subdomain IIA of HSA. This Zn(II) complex was used for the preparation of ZnO nanoparticles, and their photocatalytic activities were examined via photocatalytic degradation of ethidium bromide (EBr) in the absence of UV-vis irradiation. The results showed that these nanoparticles are promising materials for photocatalytic degradation.
合成并表征了一种使用四齿席夫碱配体的新型席夫碱 Zn(II) 配合物。细胞毒性试验结果表明，所制备的配合物在乳腺癌细胞系中诱导细胞毒性。因此，使用光谱和分子对接方法研究了 Zn(II) 配合物与人血清白蛋白 (HSA) 的结合。荧光数据表明，Zn(II) 配合物通过静态猝灭机制猝灭蛋白质荧光。计算了结合常数 (K)、结合位点数 (n) 和热力学参数，并表明 Zn(II) 配合物通过氢键和 Vander Waals 相互作用与一个结合位点结合到 HSA 上。蛋白配体对接分析证实，Zn(II) 配合物与位于 HSA 亚结构域 IIA 中的残基结合。该 Zn(II) 配合物用于制备 ZnO 纳米粒子，并通过在没有紫外-可见辐射的情况下用光催化降解溴化乙锭 (EBr) 来检查它们的光催化活性。结果表明，这些纳米粒子是用于光催化降解的有前途的材料。
