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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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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… Click to show full 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.

Keywords: carbonic anhydrase; inhibition; intermolecular amination; amination allylic; allylic benzylic

Journal Title: Journal of Biochemical and Molecular Toxicology
Year Published: 2018

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