Yayın: 1,2,3-Triazole substituted phthalocyanine metal complexes as potential inhibitors for anticholinesterase and antidiabetic enzymes with molecular docking studies
| 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 | 2026-01-04T14:44:59Z | |
| dc.date.issued | 2020-12-09 | |
| 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 (<b>2-6</b>) effectively inhibited AChE, with <i>K<sub>i</sub></i> values in the range of 40.11 ± 5.61 to 78.27 ± 15.42 µM. For α-glycosidase, the most effective <i>K<sub>i</sub></i> values of compounds <b>1</b> and <b>2</b> were with <i>K<sub>i</sub></i> 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 (<b>1</b>) and its metal complexes (<b>2</b>–<b>6</b>). Biological activities of <b>1</b> 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 | |
| dc.description.uri | https://doi.org/10.1080/07391102.2020.1857842 | |
| dc.description.uri | https://dx.doi.org/10.6084/m9.figshare.13352420.v1 | |
| dc.description.uri | https://dx.doi.org/10.6084/m9.figshare.13352420 | |
| dc.description.uri | https://pubmed.ncbi.nlm.nih.gov/33292060 | |
| dc.description.uri | https://dx.doi.org/10.1080/07391102.2020.1857842 | |
| dc.description.uri | https://hdl.handle.net/20.500.14002/388 | |
| dc.description.uri | https://hdl.handle.net/20.500.12418/13861 | |
| dc.description.uri | https://hdl.handle.net/20.500.12418/13570 | |
| dc.description.uri | http://hdl.handle.net/11772/11643 | |
| dc.description.uri | https://hdl.handle.net/11772/22889 | |
| dc.description.uri | http://hdl.handle.net/11772/9329 | |
| dc.description.uri | https://aperta.ulakbim.gov.tr/record/10181 | |
| dc.description.uri | https://doi.org/https://doi.org/20.500.12418/13861 | |
| dc.description.uri | https://doi.org/https://doi.org/10.1080/07391102.2020.1857842 | |
| dc.description.uri | https://doi.org/https://doi.org/20.500.12418/13570 | |
| dc.identifier.doi | 10.1080/07391102.2020.1857842 | |
| dc.identifier.eissn | 1538-0254 | |
| dc.identifier.endpage | 4439 | |
| dc.identifier.issn | 0739-1102 | |
| dc.identifier.openaire | doi_dedup___::fd9b988a0aae91a813521252a713ee7c | |
| dc.identifier.orcid | 0000-0001-8710-2912 | |
| dc.identifier.orcid | 0000-0002-3171-0633 | |
| dc.identifier.orcid | 0000-0002-0420-2043 | |
| dc.identifier.orcid | 0000-0002-1142-3936 | |
| dc.identifier.pubmed | 33292060 | |
| dc.identifier.scopus | 2-s2.0-85097366473 | |
| dc.identifier.startpage | 4429 | |
| dc.identifier.uri | https://hdl.handle.net/20.500.12597/38389 | |
| dc.identifier.volume | 40 | |
| dc.identifier.wos | 000597030900001 | |
| dc.language.iso | eng | |
| dc.publisher | Informa UK Limited | |
| dc.relation.ispartof | Journal of Biomolecular Structure and Dynamics | |
| dc.rights | OPEN | |
| dc.subject | Indoles | |
| dc.subject | Enzyme Inhibition | |
| dc.subject | Glycoside Hydrolases | |
| dc.subject | Dft Studies | |
| dc.subject | Isoindoles | |
| dc.subject | Structure-Activity Relationship | |
| dc.subject | DFT studies | |
| dc.subject | Coordination Complexes | |
| dc.subject | Hypoglycemic Agents | |
| dc.subject | molecular docking | |
| dc.subject | Molecular Biology | |
| dc.subject | enzyme inhibition | |
| dc.subject | Phthalocyanin etriazole enzyme inhibition molecular docking DFT studies | |
| dc.subject | Phthalocyanine | |
| dc.subject | molecular docking | |
| dc.subject | Triazoles | |
| dc.subject | Molecular Docking | |
| dc.subject | Molecular Docking Simulation | |
| dc.subject | triazole | |
| dc.subject | Acetylcholinesterase | |
| dc.subject | Triazole | |
| dc.subject | Cholinesterase Inhibitors | |
| dc.subject.sdg | 3. Good health | |
| 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 | |
| local.import.source | OpenAire | |
| local.indexed.at | WOS | |
| local.indexed.at | Scopus | |
| local.indexed.at | PubMed |
