1,2,3-Triazole substituted phthalocyanine metal complexes as potential inhibitors for anticholinesterase and antidiabetic enzymes with molecular docking studies
| dc.contributor.author | Kocyigit, Umit M. | |
| dc.contributor.author | Taslimi, Parham | |
| dc.contributor.author | Tuzun, Burak | |
| dc.contributor.author | Yakan, Hasan | |
| dc.contributor.author | Muglu, Halit | |
| dc.contributor.author | Guzel, Emre | |
| dc.contributor.author | Taslimi, Parham | |
| dc.date.accessioned | 2025-10-18T13:24:20Z | |
| dc.date.created | 2020 | |
| dc.date.issued | 2020 | |
| dc.department | Fakülteler, Fen Fakültesi, Biyoteknoloji Bölümü | |
| dc.description.abstract | In recent years, acetylcholinesterase (AChE) and alpha-glycosidase (alpha-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 K-i values in the range of 40.11 +/- 5.61 to 78.27 +/- 15.42 mu M. For alpha-glycosidase, the most effective K-i values of compounds 1 and 2 were with K-i values of 16.11 +/- 3.13 and 18.31 +/- 2.42 mu M, 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 alpha-glycosidase for ID 1R47 (alpha-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 | |
| dc.description.sponsorship | Research Fund of the Sakarya University of Applied Sciences [2020-01-10-015]; TUBITAK ULAKBIM High Performance and Grid Computing Center (TR-Grid eInfrastructure) | |
| dc.description.sponsorship | This work was supported by Research Fund of the Sakarya University of Applied Sciences (Project Number: 2020-01-10-015) and TUBITAK ULAKBIM High Performance and Grid Computing Center (TR-Grid eInfrastructure). | |
| dc.identifier.doi | 10.1080/07391102.2020.1857842 | |
| dc.identifier.endpage | 4439 | |
| dc.identifier.issn | 0739-1102 | |
| dc.identifier.issn | 1538-0254 | |
| dc.identifier.issue | 10 | |
| dc.identifier.orcid | YAKAN, HASAN/0000-0002-4428-4696 | |
| dc.identifier.orcid | Kocyigit, Umit Muhammet/0000-0001-8710-2912 | |
| dc.identifier.orcid | TUZUN, BURAK/0000-0002-0420-2043 | |
| dc.identifier.orcid | Taslimi, Parham/0000-0002-3171-0633 | |
| dc.identifier.orcid | Guzel, Emre/0000-0002-1142-3936; | |
| dc.identifier.pmid | 33292060 | |
| dc.identifier.scopus | 2-s2.0-85097366473 | |
| dc.identifier.scopusquality | Q1 | |
| dc.identifier.startpage | 4429 | |
| dc.identifier.uri | https://doi.org/10.1080/07391102.2020.1857842 | |
| dc.identifier.uri | https://hdl.handle.net/11772/22889 | |
| dc.identifier.volume | 40 | |
| dc.identifier.wos | WOS:000597030900001 | |
| dc.identifier.wosquality | N/A | |
| dc.indekslendigikaynak | Web of Science | |
| dc.indekslendigikaynak | Scopus | |
| dc.indekslendigikaynak | PubMed | |
| dc.language.iso | en | |
| dc.publisher | Taylor & Francis Inc | |
| dc.relation.ispartof | Journal of Biomolecular Structure & Dynamics | |
| dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | |
| dc.relation.sdg | Goal-03: Good Health and Well-Being | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.snmz | WoS_20251016 | |
| dc.subject | Phthalocyanine | |
| dc.subject | Triazole | |
| dc.subject | Enzyme Inhibition | |
| dc.subject | Molecular Docking | |
| dc.subject | Dft Studies | |
| dc.title | 1,2,3-Triazole substituted phthalocyanine metal complexes as potential inhibitors for anticholinesterase and antidiabetic enzymes with molecular docking studies | |
| dc.type | Article | |
| dspace.entity.type | Publication | |
| relation.isAuthorOfPublication | dadfa319-65b8-4543-92b4-bea49e0139e9 | |
| relation.isAuthorOfPublication.latestForDiscovery | dadfa319-65b8-4543-92b4-bea49e0139e9 |










