Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes |
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| Authors: | Ufuk Atmaca Alper Y?ld?r?m Parham Taslimi Seda Tuncel Çelik ?lhami Gülçin Claudiu T Supuran Murat Çelik |
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| Institution: | 1. Department of Chemistry, Faculty of Science, Ataturk University, Erzurum‐Turkey;2. Dipartimento Di ChimicaUgo Schiff, Universita DegliStudi Di Firenze, Firenze, Italy;3. Department of Neurofarba, Section of Pharmaceutical and Nutriceutical Sciences, Universita DegliStudi Di Firenze, Florence, Italy |
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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. |
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| Keywords: | acetylcholinesterase amination carbonic anhydrase sulfamate sulfonamide |
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