Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes. Issue 8 (5th July 2018)

• Record Type: Journal Article
• Authors: Atmaca, Ufuk; Yıldırım, Alper; Taslimi, Parham; Çelik, Seda Tuncel; Gülçin, İlhami; Supuran, Claudiu T.; Çelik, Murat
• Is Part Of: Journal of biochemical and molecular toxicology. Volume 32:Issue 8(2018)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2018-07-05
• Subjects: acetylcholinesterase -- amination -- carbonic anhydrase -- sulfamate -- sulfonamide; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Toxicology -- Periodicals; 574
• DOI: 10.1002/jbt.22173
• Languages: English
• ISSNs: 1095-6670

Abstract

Abstract: In this study, we aimed to determine the inhibition effects of novel synthesized sulfamates (2a–g ), sulfonamides (3b–f ), carbonyl sulfonamides (3h andi ), and carbonyl sulfamates (4h and4i ), 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.