Department of Chemistry, Faculty of Science, Ataturk University, 25240, Erzurum-Turkey.
Dipartimento Di ChimicaUgo Schiff, Universita DegliStudi Di Firenze, Firenze, Italy.
J Biochem Mol Toxicol. 2018 Aug;32(8):e22173. doi: 10.1002/jbt.22173. Epub 2018 Jul 5.
In this study, we aimed to determine the inhibition effects of novel synthesized sulfamates (2a-g), sulfonamides (3b-f), carbonyl sulfonamides (3h and i), and carbonyl sulfamates (4h and 4i), which were tested against two human cytosolic carbonic anhydrase I and II isozymes (hCA I and II) and acetylcholinesterase (AChE) enzyme. For inhibition properties of allylic sulfamates, the half maximal inhibitory concentration (IC ) and inhibition constant (K ) were calculated for each novel compounds. The allylic sulfamates showed that K values are in the range of 187.33-510.31 pM for hCA I, 104.22-290.09 pM against hCA II, and 12.73-103.63 pM against AChE. The results demonstrated that all newly synthesized compounds had shown effective inhibition against hCA I and II isoenzymes and AChE enzyme.
在这项研究中，我们旨在确定新型合成的磺胺酸盐（2a-g）、磺胺类药物（3b-f）、羰基磺胺类药物（3h 和 i）和羰基磺胺酸盐（4h 和 4i）对两种人细胞质碳酸酐酶 I 和 II 同工酶（hCA I 和 II）和乙酰胆碱酯酶（AChE）的抑制作用。对于烯丙基磺胺酸盐的抑制特性，我们计算了每个新化合物的半最大抑制浓度（IC ）和抑制常数（K ）。烯丙基磺胺酸盐的结果表明，K 值范围为 187.33-510.31 pM 针对 hCA I，104.22-290.09 pM 针对 hCA II，12.73-103.63 pM 针对 AChE。结果表明，所有新合成的化合物均对 hCA I 和 II 同工酶以及 AChE 酶表现出有效的抑制作用。
