| Yazarlar |
Ümit M. Koçyiğit
|
|
Parham Taslımı
Türkiye |
|
Burak Tüzün
Türkiye |
|
Hasan Yakan
Türkiye |
Doç. Dr. Halit MUĞLU
Türkiye |
|
Emre Güzel
Türkiye |
| Özet |
| In recent years, acetylcholinesterase (AChE) and α-glycosidase (α-gly) inhibition have emerged as a promising and important approach for pharmacological intervention in many diseases such as glaucoma, epilepsy, obesity, cancer, and Alzheimer's. In this manner, the preparation and enzyme inhibition activities of peripherally 1,2,3-triazole group substituted metallophthalocyanine derivatives with strong absorption in the visible region were presented. These novel metallophthalocyanine derivatives (2-6) effectively inhibited AChE, with Ki values in the range of 40.11 ± 5.61 to 78.27 ± 15.42 µM. For α-glycosidase, the most effective Ki values of compounds 1 and 2 were with Ki values of 16.11 ± 3.13 and 18.31 ± 2.42 µM, respectively. Also, theoretical calculations were investigated to compare the chemical and biological activities of the ligand (1) and its metal complexes (2–6). Biological activities of 1 and its complexes against acetylcholinesterase for ID 4M0E (AChE) and α-glycosidase for ID 1R47 (α-gly) are calculated. Theoretical calculations were compatible with the experimental results and these 1,2,3-triazole substituted phthalocyanine metal complexes were found to be efficient inhibitors for anticholinesterase and antidiabetic enzymes. Communicated by Ramaswamy H. Sarma. |
| Anahtar Kelimeler |
| DFT studies | enzyme inhibition | molecular docking | Phthalocyanine | triazole |
| Makale Türü | Özgün Makale |
| Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale |
| Dergi Adı | Journal of Biomolecular Structure and Dynamics |
| Dergi ISSN | 0739-1102 |
| Dergi Tarandığı Indeksler | SCI-Expanded |
| Dergi Grubu | Q2 |
| Makale Dili | Türkçe |
| Basım Tarihi | 05-2022 |
| Cilt No | 40 |
| Sayı | 10 |
| Sayfalar | 4429 / 4439 |
| Doi Numarası | 10.1080/07391102.2020.1857842 |
| Makale Linki | http://dx.doi.org/10.1080/07391102.2020.1857842 |
| Atıf Sayıları | |
| SCOPUS | 30 |
