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 | 2023-04-12T05:27:10Z | |
dc.date.available | 2023-04-12T05:27:10Z | |
dc.date.issued | 09.12.2020 | tr |
dc.identifier.citation | Umit M. Koc € ¸yigit a , Parham Taslimib , Burak Tuz€ un€ c , Hasan Yakand
, Halit Muglu e and Emre Guzel € f
a
Department of Basic Pharmaceutical Sciences, Sivas Cumhuriyet University, Sivas, Turkey; b
Department of Biotechnology, Faculty of
Science, Bartın University, Bartin, Turkey; c
Department of Chemistry, Sivas Cumhuriyet University, Sivas, Turkey; d
Department of Chemistry
Education, Ondokuz Mayıs University, Samsun, Turkey; e
Department of Chemistry, Kastamonu University, Kastamonu, Turkey; f
Department
of Fundamental Sciences, Faculty of Technology, Sakarya University of Applied Sciences, Sakarya, Turkey
Communicated by Ramaswamy H. Sarma | tr |
dc.identifier.uri | https://hdl.handle.net/20.500.12418/13570 | |
dc.description.abstract | In recent years, acetylcholinesterase (AChE) and a-glycosidase (a-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 mM. For
a-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 mM, 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 a-glycosidase for ID 1R47
(a-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.language.iso | eng | tr |
dc.relation.isversionof | https://doi.org/10.1080/07391102.2020.1857842 | tr |
dc.rights | info:eu-repo/semantics/openAccess | tr |
dc.subject | enzyme inhibition | tr |
dc.subject | ; molecular docking | tr |
dc.subject | DFT studies | tr |
dc.subject | triazole | tr |
dc.subject | Phthalocyanine | 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 ISSN | tr |
dc.contributor.department | Sivas Meslek Yüksekokulu | tr |
dc.contributor.authorID | https://orcid.org/0000-0002-0420-2043 | tr |
dc.contributor.authorID | 1 | tr |
dc.identifier.volume | 40 | tr |
dc.identifier.issue | 10 | tr |
dc.identifier.endpage | 4439 | tr |
dc.identifier.startpage | 4429 | tr |
dc.relation.publicationcategory | Uluslararası Editör Denetimli Dergide Makale | tr |