| Title : Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes - Atmaca_2018_J.Biochem.Mol.Toxicol__e22173 |
| Author(s) : Atmaca U , Yildirim A , Taslimi P , Celik ST , Gulcin I , Supuran CT , Celik M |
| Ref : J Biochem Mol Toxicol , :e22173 , 2018 |
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Abstract :
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 (IC50 ) and inhibition constant (Ki ) were calculated for each novel compounds. The allylic sulfamates showed that Ki 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. |
| PubMedSearch : Atmaca_2018_J.Biochem.Mol.Toxicol__e22173 |
| PubMedID: 29975450 |
Atmaca U, Yildirim A, Taslimi P, Celik ST, Gulcin I, Supuran CT, Celik M (2018)
Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes
J Biochem Mol Toxicol
:e22173
Atmaca U, Yildirim A, Taslimi P, Celik ST, Gulcin I, Supuran CT, Celik M (2018)
J Biochem Mol Toxicol
:e22173