Synthesis, characterization, crystal structures, theoretical calculations and biological evaluations of novel substituted tacrine derivatives as cholinesterase and carbonic anhydrase enzymes inhibitors
Yükleniyor...
Tarih
2019
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Elsevier Science Bv
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
The six and seven hydrocycle membered disilylanilino acridine (tacrine) analogues (9-11) were synthesized by one-pot procedures. The structures of novel silyl tacrine derivatives were characterized by NMR spectroscopy, elemental analysis and XRD investigations. The silyl substituted novel tacrine derivatives (9-11) were investigated as cholinesterase inhibitors and defined the relative role of AChE (Acetylcholinesterase) versus BChE (Butyrylcholinesterase) inhibition. Novel substituted tacrine derivatives are known as important inhibitors of Carbonic anhydrase (CA) isoenzymes I, and II (hCA I and II), therefore, the synthesized compounds (9-11) were investigated for inhibitory effects on the both CA isoenzymes. Additionally, we evaluated four different enzymes, which were inhibited in the very low nanomolar (nM) range by these compounds. According to the present studies, for AChE, BChE, hCA I and II, the ranges of results are recorded as 30.26 +/- 6.71-117.54 +/- 42.22 nM, 22.45 +/- 5.81-77.41 +/- 4.02 nM, 57.28 +/- 22.16-213.41 +/- 82.75 nM and 46.95 +/- 11.32-274.94 +/- 62.15 nM, respectively. (C) 2018 Elsevier B.V. All rights reserved.
Açıklama
Okten, Salih/0000-0001-9656-1803; GULCIN, Ilhami/0000-0001-5993-1668;
Anahtar Kelimeler
Silyl tacrine, Deprotonation of amine, Acetylcholinesterase, Butyrylcholinesterase, Carbonic anhydrase, Enzyme inhibitor
Kaynak
Journal Of Molecular Structure
WoS Q Değeri
Q3
Scopus Q Değeri
Q1
Cilt
1175
Sayı
Künye
closedAccess
