Synthesis, characterization of novel mannich bases and their acetylcholinesterase and glutathione S-transferase inhibitory properties: An in vitro and in silico mechanism research
Yazarlar (8)
Dr. Öğr. Üyesi Gül ÖZDEMİR TORAMAN
Kafkas Üniversitesi, Türkiye
Alpaslan Bayrakdar
Iğdır Üniversitesi, Türkiye
Ercan Oğuz
Iğdır Üniversitesi, Türkiye
Doç. Dr. Murat BEYTUR
Kafkas Üniversitesi, Türkiye
Fikret Türkan
Iğdır Üniversitesi, Türkiye
Doç. Dr. Sevda MANAP
Kafkas Üniversitesi, Türkiye
Abdülmelik Aras
Iğdır Üniversitesi, Türkiye
Prof. Dr. Haydar YÜKSEK
Kafkas Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Journal of Molecular Structure (Q2) | ||
| Dergi ISSN | 0022-2860 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | Türkçe | Basım Tarihi | 02-2025 |
| Cilt / Sayı / Sayfa | 1321 / 1 / 1–10 | DOI | 10.1016/j.molstruc.2024.139733 |
| Makale Linki | https://doi.org/10.1016/j.molstruc.2024.139733 | ||
| Özet |
| In this study, 4-((3,4-Dimethoxybenzylidene)amino)-5-alkyl(aryl)-2,4-dihydro-3H-1,2,4-triazol-3-ones (4a-g) reacted with formaldehyde and 2,6-dimethylmorpholine to obtain seven novel potential biologically active 4-((3,4-Dimethoxybenzylidene)amino)-2-((2,6-dimethylmorpholino)methyl)-5-alkyl(aryl)-2,4-dihydro-3H-1,2,4-triazol-3-ones (5a-g). The structures (5a-g) of newly synthesized compounds were characterized using FT-IR, 1H-NMR, and 13C-NMR spectral data. The synthesized compounds (5a-g) were investigated for it is in vitro enzyme inhibition properties. Results demonstrated that the newly synthesized compounds had valuable enzyme inhibition activities against acetylcholinesterase (AChE) and glutathione S-transferase (GST) enzymes. Their Ki values were calculated in the range of 0.96 ± 0.0557- 9.7967 ± 5.3105 µM, while their IC50 values were calculated in the range of 1.333–3.551 µM. Tacrine was used for AChE, Ethacrynic acid was used for GST as positive standard. Molecular docking studies revealed that compound 5b binds to AChE and compound 5f binds to GST with high affinity (−10.2 and −9.1 kcal/mol) in protein-ligand complexes. The stability of the ligand-protein complexes was confirmed by 100 ns molecular dynamics simulations. |
| Anahtar Kelimeler |
| 4,5-Dihydro-1H-1,2,4-triazol-5-one | Enzyme inhibition | Mannich base | Molecular dynamics | Schiff base | Synthesis |
Science Direct
Synthesis, characterization of novel mannich bases and their acetylcholinesterase and glutathione S-transferase inhibitory properties: An in vitro and in silico mechanism research
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| SCOPUS | 10 |
| Google Scholar | 10 |