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Discovery of potent carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase enzymes inhibitors: The new amides and thiazolidine‐4‐ones synthesized on an acetophenone base
Author(s) -
Taslimi Parham,
Osmanova Sabiya,
Gulçin İlhami,
Sardarova Sabira,
Farzaliyev Vagif,
Sujayev Afsun,
Kaya Ruya,
Koc Fatma,
Beydemir Sukru,
Alwasel Saleh H.,
Kufrevioglu Omer Irfan
Publication year - 2017
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.21931
Subject(s) - butyrylcholinesterase , chemistry , acetylcholinesterase , carbonic anhydrase , thiazolidine , cholinesterase , enzyme , aché , carbonic anhydrase i , tacrine , pyrroline , stereochemistry , biochemistry , carbonic anhydrase ii , pharmacology , medicine
Compounds containing nitrogen and sulfur atoms can be widely used in various fields, including industry, medicine, biotechnology, and chemical technology. Among them, amides of acids and heterocyclic compounds have an important place. These amides and thiazolidine‐4‐ones showed good inhibitory action against butyrylcholinesterase (BChE), acetylcholinesterase (AChE), and human carbonic anhydrase isoforms. AChE exists at high concentrations in the brain and red blood cells. BChE is an important enzyme that is plentiful in the liver, and it is released into the blood in a soluble form. They were demonstrated to have effective inhibition profiles with K i values of 23.76–102.75 nM against hCA I, 58.92–136.64 nM against hCA II, 1.40–12.86 nM against AChE, and 9.82–52.77 nM against BChE. On the other hand, acetazolamide showed K i value of 482.63 ± 56.20 nM against hCA I, and 1019.60 ± 163.70 nM against hCA II. Additionally, Tacrine inhibited AChE and BChE, showing K i values of 397.03 ± 31.66 and 210.21 ± 15.98 nM, respectively.