Pubmed: 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 | 2023-04-07T00:03:42Z | |
dc.date.available | 2023-04-07T00:03:42Z | |
dc.date.issued | 2022-07-01T00:00:00Z | |
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 () effectively inhibited AChE, with values in the range of 40.11 ± 5.61 to 78.27 ± 15.42 µM. For α-glycosidase, the most effective values of compounds and were with 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 () and its metal complexes (-). Biological activities of 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.identifier.doi | 10.1080/07391102.2020.1857842 | |
dc.identifier.issn | 1538-0254 | |
dc.identifier.pubmed | 33292060 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12597/3419 | |
dc.language.iso | en | |
dc.relation.ispartof | Journal of biomolecular structure & dynamics | |
dc.subject | DFT studies | |
dc.subject | Phthalocyanine | |
dc.subject | enzyme inhibition | |
dc.subject | molecular docking | |
dc.subject | triazole | |
dc.title | 1,2,3-Triazole substituted phthalocyanine metal complexes as potential inhibitors for anticholinesterase and antidiabetic enzymes with molecular docking studies. | |
dc.type | Journal Article | |
dc.type | Research Support, Non-U.S. Gov't | |
dspace.entity.type | Pubmed | |
oaire.citation.issue | 10 | |
oaire.citation.volume | 40 | |
relation.isPublicationOfPubmed | 7dca511e-d879-46fc-ac56-74cca78eb202 | |
relation.isPublicationOfPubmed.latestForDiscovery | 7dca511e-d879-46fc-ac56-74cca78eb202 |