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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
Author(s) -
Atmaca Ufuk,
Yıldırım Alper,
Taslimi Parham,
Çelik Seda Tuncel,
Gülçin İlhami,
Supuran Claudiu T.,
Çelik Murat
Publication year - 2018
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.22173
Subject(s) - chemistry , acetylcholinesterase , carbonic anhydrase , carbonic anhydrase i , allylic rearrangement , enzyme , isozyme , stereochemistry , amination , active site , medicinal chemistry , biochemistry , catalysis
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 50 ) and inhibition constant ( K i ) were calculated for each novel compounds. The allylic sulfamates showed that K i 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.