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dc.contributor.authorTaslimi, P. and Caglayan, C. and Farzaliyev, V. and Nabiyev, O. and Sujayev, A. and Turkan, F. and Kaya, R. and Gulçin, İ.
dc.date.accessioned2021-04-08T12:07:18Z
dc.date.available2021-04-08T12:07:18Z
dc.date.issued2018
dc.identifier10.1002/jbt.22042
dc.identifier.issn10956670
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85045911804&doi=10.1002%2fjbt.22042&partnerID=40&md5=028f4ec8bddd29986135f600ee8cf55f
dc.identifier.urihttp://acikerisim.bingol.edu.tr/handle/20.500.12898/4291
dc.description.abstractDuring this investigation, N,N′-bis-azidomethylamines, N,N′-bis-cyanomethylamine, new alkoxymethylamine and chiral derivatives, which are considered to be a new generation of multifunctional compounds, were synthesized, functional properties were investigated, and anticholinergic and antidiabetic properties of those compounds were studied through the laboratory tests, and it was approved that they contain physiologically active compounds rather than analogues. Novel N-bis-cyanomethylamine and alkoxymethylamine derivatives were effective inhibitors of the α-glycosidase, cytosolic carbonic anhydrase I and II isoforms, butyrylcholinesterase (BChE), and acetylcholinesterase (AChE) with Ki values in the range of 0.15–13.31 nM for α-glycosidase, 2.77–15.30 nM for human carbonic anhydrase isoenzymes I (hCA I), 3.12–21.90 nM for human carbonic anhydrase isoenzymes II (hCA II), 23.33–73.23 nM for AChE, and 3.84–48.41 nM for BChE, respectively. Indeed, the inhibition of these metabolic enzymes has been considered as a promising factor for pharmacologic intervention in a diversity of disturbances. © 2018 Wiley Periodicals, Inc.
dc.language.isoEnglish
dc.sourceJournal of Biochemical and Molecular Toxicology
dc.titleSynthesis and discovery of potent carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α-glycosidase enzymes inhibitors: The novel N,N′-bis-cyanomethylamine and alkoxymethylamine derivatives


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