Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes
Özet
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 (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.
Anahtar kelimeler
Atıf için künye
Atmaca, U., Yıldırım, A., Taslimi, P., Çelik, S. T., Gülçin, İ., Supuran, C. T., & Çelik, M. (2018). Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes. JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, 32(8). https://doi.org/10.1002/jbt.22173
BibTeX
@article{atmaca2018-67895,
author = {Atmaca, Ufuk and Yıldırım, Alper and Taslimi, Parham and Çelik, Seda Tuncel and Gülçin, İlhami and Supuran, Claudiu T. and Çelik, Murat},
title = {Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes},
journal = {JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY},
year = {2018},
volume = {32},
number = {8},
issn = {1095-6670},
doi = {10.1002/jbt.22173},
url = {https://akademik.atauni.edu.tr/yayinlar/67895-intermolecular-amination-of-allylic-and-benzylic-alcohols-leads-to-effective}
}