Synthesis, Spectroscopic Analysis, and in Vitro/in Silico Biological Studies of Novel Piperidine Derivatives Heterocyclic Schiff‐Mannich Base Compounds
Yazarlar (8)
Songül Boy Türkiye
Abdülmelik Aras Iğdır Üniversitesi, Türkiye
Fikret Türkkan
Türkiye
Türkiye
Doç. Dr. Onur AKYILDIRIM Kafkas Üniversitesi, Türkiye
Doç. Dr. Murat BEYTUR Kafkas Üniversitesi, Türkiye
Sedef Karaman
Türkiye
Türkiye
Doç. Dr. Sevda MANAP Kafkas Üniversitesi, Türkiye
Prof. Dr. Haydar YÜKSEK Kafkas Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Chemistry & Biodiversity (Q3) | ||
| Dergi ISSN | 1612-1872 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | Türkçe | Basım Tarihi | 01-2021 |
| Cilt / Sayı / Sayfa | 18 / 0 / – | DOI | 10.1002/cbdv.202100433 |
| Makale Linki | http://dx.doi.org/10.1002/cbdv.202100433 | ||
| Özet |
| AbstractIn the present study, 3‐substitued‐4‐(4‐hydroxybenzylidenamino)‐4,5‐dihydro‐1H‐1,2,4‐triazol‐5‐ones (S1‐8) were synthesized by treating 4‐hydroxybenzaldehyde (B) with eight different 3‐substitued‐4‐amino‐4,5‐dihydro‐1H‐1,2,4‐triazole‐5‐ones (T1‐8) in acetic acid medium, separately. The synthesized Schiff bases (S) were reacted with formaldehyde and secondary amine such as 4‐piperidinecarboxyamide to afford novel heterocyclic bases. 3‐Substitued‐4‐(4‐hydroxybenzylidenamino)‐4,5‐dihydro‐1H‐1,2,4‐triazol‐5‐ones (T) were treated with 4‐piperidinecarboxyamide in the presence of formaldehyde to synthesize eight new 1‐(4‐piperidinecarboxyamide‐1‐yl‐methyl)‐3‐substitued‐4‐(4‐hydroxybenzylidenamino)‐4,5‐dihydro‐1H‐1,2,4‐triazol‐5‐ones (M1‐8). The structure characterization of compounds was carried out using 1H‐NMR, IR, HR‐MS, and 13C‐NMR spectroscopic methods. The inhibitory properties of the newly synthesized compounds were calculated against the acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and glutathione S‐transferase (GST) enzymes. Ki values were calculated in the range of 20.06±3.11–36.86±6.17 μM for GST, 17.87±2.91–30.53±4.25 μM for AChE, 9.08±0.69–20.02±2.88 μM for BChE, respectively, Besides, IC50 values were also calculated. Best binding scores of ‐inhibitors against used enzymes were calculated as −12.095 kcal/mol, −12.775 kcal/mol, and −9.336 kcal/mol, respectively. While 5‐oxo‐triazole piperidine‐4‐carboxamide moieties have a critical role in the inhibition of AChE and GST enzymes, hydroxy benzyl moiety is important for BChE enzyme inhibition. |
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