dc.contributor.author | Koçyiğit,Ümit M. | |
dc.contributor.author | Taslimi, Parham | |
dc.contributor.author | Tüzün,Burak | |
dc.contributor.author | Yakan,Hasan | |
dc.contributor.author | Muğlu, Halit | |
dc.contributor.author | Güzel,Emre | |
dc.date.accessioned | 2023-06-21T13:21:51Z | |
dc.date.available | 2023-06-21T13:21:51Z | |
dc.date.issued | 2022/01/26 | tr |
dc.identifier.uri | https://hdl.handle.net/20.500.12418/13861 | |
dc.description.abstract | 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. | tr |
dc.publisher | Taylor & Francis | tr |
dc.relation.isversionof | 10.1080/07391102.2020.1857842 | tr |
dc.rights | info:eu-repo/semantics/openAccess | tr |
dc.subject | Phthalocyanin etriazole enzyme inhibition molecular docking DFT studies | tr |
dc.title | 1, 2, 3-Triazole substituted phthalocyanine metal complexes as potential inhibitors for anticholinesterase and antidiabetic enzymes with molecular docking studies | tr |
dc.type | article | tr |
dc.relation.journal | Journal of Biomolecular Structure and Dynamics | tr |
dc.contributor.department | Eczacılık Fakültesi | tr |
dc.contributor.authorID | 0000-0001-8710-2912 | tr |
dc.identifier.volume | 40 | tr |
dc.identifier.issue | 10 | tr |
dc.identifier.endpage | 4439 | tr |
dc.identifier.startpage | 4429 | tr |
dc.relation.publicationcategory | Ulusal Hakemli Dergide Makale - Kurum Öğretim Elemanı | tr |