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Synthesis of new cyclic thioureas and evaluation of their metal‐chelating activity, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibition profiles
Author(s) -
Taslimi Parham,
Sujayev Afsun,
Garibov Emin,
Nazarov Nazar,
Huyut Zubeyir,
Alwasel Saleh H.,
Gulçin İlhami
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.21897
Subject(s) - butyrylcholinesterase , chemistry , acetylcholinesterase , carbonic anhydrase , thiourea , cholinesterase , aché , tacrine , acetazolamide , chelation , stereochemistry , enzyme , nuclear chemistry , organic chemistry , pharmacology , medicine
In the presence of trifluoracetic acid (TFAA), an efficient method for the synthesis of tetra(hexa)hydropyrimidinethione‐carboxylates has been used on the basis of three‐component condensation of thiourea with its different aldehydes and β‐diketones. Some novel cyclic thioureas were synthesized, and their hCA I, hCA II, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) inhibitors and metal‐chelating properties were evaluated. K i values of novel synthesized compounds for AChE and BChE are in the range of 51.84–135.96 and 143.96–274.55 nM, respectively. Also, HCA I and II were effectively inhibited by these novel compounds, with K i values in the range of 404.16–745.13 nM for hCA I and of 434.20–689.57 nM for hCA II, respectively. Additionally, acetazolamide (AZA), clinically used as a CA inhibitor, with a K i value of 883.68 ± 121.27 nM in hCA I and 1008.66 ± 144.70 nM in hCA II. Also, tacrine inhibited AChE and BChE showed K i values of 314.63 ± 31.66 and 373.57 ± 75.07 nM, respectively.