Synthesis, design, and assessment of novel morpholine-derived Mannich bases as multifunctional agents for the potential enzyme inhibitory properties including docking study
 
Yazarlar (7)
Dr. Öğr. Üyesi Songül BOY Kafkas Üniversitesi, Türkiye
Fikret Türkan Iğdır Üniversitesi, Türkiye
Doç. Dr. Murat BEYTUR Kafkas Üniversitesi, Türkiye
Abdülmelik Aras Iğdır Üniversitesi, Türkiye
Doç. Dr. Onur AKYILDIRIM Kafkas Üniversitesi, Türkiye
Halide Sedef Karaman Atatürk Üniversitesi, Türkiye
Prof. Dr. Haydar YÜKSEK Kafkas Üniversitesi, Türkiye
Makale Türü Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Bioorganic Chemistry (Q1)
Dergi ISSN 0045-2068 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce Basım Tarihi 02-2021
Cilt / Sayı / Sayfa 107 / 1 / 1–8 DOI 10.1016/j.bioorg.2020.104524
Makale Linki http://dx.doi.org/10.1016/j.bioorg.2020.104524
Özet
The synthesized Schiff Bases were reacted with formaldehyde and secondary amine such as 2,6-dimethylmorpholine to afford N-Mannich bases through the Mannich reaction. 3-Substitued-4-(4-hydroxybenzylidenamino)-4,5-dihydro-1H-1,2,4-triazol-5-ones (4) were treated with 2,6-dimethylmorpholine in the presence of formaldehyde to synthesize eight new 1-(2,6-dimethylmorpholino-4-yl-methyl)-3-substitued-4-(4-hydroxybenzylidenamino)-4,5-dihydro-1H-1,2,4-triazol-5-ones (4a-h). The structures of the synthesized eight new compounds were characterized using IR, 1H NMR, 13C NMR, and HR-MS spectroscopic methods. Synthesized compounds inhibitory activity determined against the acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and glutathione S-transferase (GST) enzymes with Ki values in the range 25.23–42.19 µM for AChE, 19.37–34.22 µM for BChE, and 21.84–41.14 µM for GST …
Anahtar Kelimeler
Docking | Enzyme inhibitory | Mannich bases | Morpholine | Schiff base