Novel amino acid Schiff base Zn(II) complexes as new therapeutic approaches in diabetes and Alzheimer's disease: Synthesis, characterization, biological evaluation, and molecular docking studies
Yazarlar (6)
Doç. Dr. Ayşegül ŞENOCAK
Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Bartin Üniversitesi, Türkiye
Cumhuriyet Üniversitesi, Türkiye
Bozok Üniversitesi, Türkiye
Bozok Üniversitesi, Türkiye
| Makale Türü | Özgün Makale |
| Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale |
| Dergi Adı | Journal of Biochemical and Molecular Toxicology |
| Dergi ISSN | 1095-6670 Wos Dergi Scopus Dergi |
| Dergi Tarandığı Indeksler | SCI-Expanded |
| Dergi Grubu | Q3 |
| Makale Dili | İngilizce |
| Basım Tarihi | 03-2022 |
| Cilt No | 36 |
| Sayı | 3 |
| Sayfalar | 22969 / 0 |
| DOI Numarası | 10.1002/jbt.22969 |
| Makale Linki | http://dx.doi.org/10.1002/jbt.22969 |
| Özet |
| Schiff bases are compounds that have gained importance in the paint industry due to their colorful nature and in the field of chemistry and biochemistry due to their biological activities. Various biological applications of Schiff bases, such as antitumor, antifungal, antibacterial, antioxidant, antituberculosis, and anthelmintic, have been widely studied. Within the scope of the study, 5-bromo-2-hydroxybenzaldehyde and amino acid methyl esters (isoleucine, phenylalanine, and methionine) and amino acid Schiff bases were synthesized first. The synthesis of the new Zn(II) complexes of these Schiff bases was carried out by the reaction of synthesized Schiff bases and Zn(OAc)2·2H2O. The structures of the synthesized complexes were elucidated using elemental analysis, Fourier transform infrared, nuclear magnetic resonance, UV-visible, and thermal analysis spectroscopy techniques. These synthesized salts were found to be effective inhibitor compounds for the α-glycosidase, and acetylcholinesterase enzyme with Ki values in the range of 30.50 ± 3.82–38.17 ± 6.26 µM for α-glycosidase, 3.68 ± 0.54–10.27 ± 1.68 µM for butyrylcholinesterase, and 6.26 ± 0.83–15.73 ± 4.73 µM for acetylcholinesterase, respectively. |
| Anahtar Kelimeler |
| amino acid Schiff base | enzyme inhibition | molecular docking | Zn(II) complexes |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| SCOPUS | 26 |
| Google Scholar | 30 |