Taslimi Parham, Türkan Fikret, Güngördü Solğun Derya, Aras Abdülmelik, Erden Yavuz, Celebioglu Hasan Ufuk, Tuzun Burak, Ağırtaş Mehmet Salih, Günay Sevilay, Gulcin Ilhami
Department of Biotechnology, Faculty of Science, Bartin University, Bartin, Turkey.
Health Services Vocational School, Igdır University, Igdır, Turkey.
J Biomol Struct Dyn. 2022 Apr;40(7):2991-3002. doi: 10.1080/07391102.2020.1844051. Epub 2020 Nov 24.
The compounds (-) used in this study were re-synthesized in accordance with our previous study. The inhibitory effect of the complexes on some metabolic enzymes was examined and it was demonstrated that the enzymes inhibited by ligands and their complex molecules at micromolar level. The best Ki value for α-glycosidase enzyme was absorved 1.01±0.08 µM for compound . The biological activity of ligand and metal complexes against enzymes was compared with molecular docking method. The enzymes used against ligand and metal complexes respectively: Achethylcholinesterase for ID 4M0E (AChE), butyrylcholinesterase for ID 5NN0 (BChE), α-glycosidase for ID 1XSI (α-Gly). ADME analysis was performed to examine the drug properties of the compounds (-). Besides, the anticancer properties of the complexes were studied. The doses of all compounds caused significant reductions in MCF-7 cell viability. The and compounds administered to PC-3 cells exhibited a more pronounced cytotoxic effect than the other two compounds ( and ). Furthermore, antibacterial activities of these compounds against and were examined.Communicated by Ramaswamy H. Sarma.
本研究中使用的化合物（-）是根据我们之前的研究重新合成的。研究了这些配合物对某些代谢酶的抑制作用，结果表明，这些配体及其配合物分子在微摩尔水平上对酶有抑制作用。化合物对α-糖苷酶的最佳Ki值为1.01±0.08μM。采用分子对接方法比较了配体和金属配合物对酶的生物活性。分别针对配体和金属配合物使用的酶：ID为4M0E的乙酰胆碱酯酶（AChE）、ID为5NN0的丁酰胆碱酯酶（BChE）、ID为1XSI的α-糖苷酶（α-Gly）。进行了ADME分析以研究化合物（-）的药物性质。此外，还研究了配合物的抗癌特性。所有化合物的剂量均导致MCF-7细胞活力显著降低。给予PC-3细胞的化合物和比其他两种化合物（和）表现出更明显的细胞毒性作用。此外，还检测了这些化合物对和的抗菌活性。由Ramaswamy H. Sarma传达。
