Department of the Azerbaijan National Academy of Sciences, Institute of Ecology and Natural Resources, Ganja, Azerbaijan.
Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, Turkey.
J Biochem Mol Toxicol. 2018 Sep;32(9):e22197. doi: 10.1002/jbt.22197. Epub 2018 Jul 25.
[Ni(C H N O ) (H O) ]•3(C H NO) (1) and [Co(C H N O ) (H O) ]•3(C H NO) (2) are synthesized and characterized by elemental analysis, FT-IR spectra, magnetic susceptibility, and thermal analysis. In addition, the crystal structure of Ni(II) complex is presented. Both complexes show distorted octahedral geometry. In 1 and 2, metal ions are coordinated by two oxygen atoms of salicylic residue and two nitrogen atoms of maleic amide residue from two ligands, and two oxygen atoms from two water molecules. In this paper, both compounds showed excellent inhibitory effects against human carbonic anhydrase (hCA) isoforms I, and II, α-glycosidase, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). Compounds 1 and 2 had Ki values of 18.36 ± 4.38 and 26.61 ± 7.54 nM against hCA I and 13.81 ± 3.02 and 29.56 ± 6.52 nM against hCA II, respectively. On the other hand, their Ki values were found to be 487.45 ± 54.18 and 453.81 ± 118.61 nM against AChE and 199.21 ± 50.35 and 409.41 ± 6.86 nM against BChE, respectively.
[Ni(C₅H₅N₃O₆)(H₂O)]·3(C₅H₅NO) 和 [Co(C₅H₅N₃O₆)(H₂O)]·3(C₅H₅NO) 是通过元素分析、傅里叶变换红外光谱、磁化率和热分析合成和表征的。此外,还呈现了 Ni(II) 配合物的晶体结构。两个配合物均呈现扭曲的八面体几何形状。在 1 和 2 中,金属离子由来自两个配体的水杨酸残基的两个氧原子和马来酰亚胺酰胺残基的两个氮原子以及两个水分子的两个氧原子配位。在本文中,这两种化合物均对人碳酸酐酶(hCA)同工酶 I 和 II、α-糖苷酶、乙酰胆碱酯酶(AChE)和丁酰胆碱酯酶(BChE)表现出优异的抑制作用。化合物 1 和 2 对 hCA I 的 Ki 值分别为 18.36 ± 4.38 和 26.61 ± 7.54 nM,对 hCA II 的 Ki 值分别为 13.81 ± 3.02 和 29.56 ± 6.52 nM。另一方面,它们对 AChE 的 Ki 值分别为 487.45 ± 54.18 和 453.81 ± 118.61 nM,对 BChE 的 Ki 值分别为 199.21 ± 50.35 和 409.41 ± 6.86 nM。