1,2,3-Triazole substituted phthalocyanine metal complexes as potential inhibitors for anticholinesterase and antidiabetic enzymes with molecular docking studies

dc.contributor.authorKocyigit, Umit M.
dc.contributor.authorTaslimi, Parham
dc.contributor.authorTuzun, Burak
dc.contributor.authorYakan, Hasan
dc.contributor.authorMuglu, Halit
dc.contributor.authorGuzel, Emre
dc.contributor.authorTaslimi, Parham
dc.date.accessioned2025-10-18T13:24:20Z
dc.date.created2020
dc.date.issued2020
dc.departmentFakülteler, Fen Fakültesi, Biyoteknoloji Bölümü
dc.description.abstractIn 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.sponsorshipResearch 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.sponsorshipThis 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.doi10.1080/07391102.2020.1857842
dc.identifier.endpage4439
dc.identifier.issn0739-1102
dc.identifier.issn1538-0254
dc.identifier.issue10
dc.identifier.orcidYAKAN, HASAN/0000-0002-4428-4696
dc.identifier.orcidKocyigit, Umit Muhammet/0000-0001-8710-2912
dc.identifier.orcidTUZUN, BURAK/0000-0002-0420-2043
dc.identifier.orcidTaslimi, Parham/0000-0002-3171-0633
dc.identifier.orcidGuzel, Emre/0000-0002-1142-3936;
dc.identifier.pmid33292060
dc.identifier.scopus2-s2.0-85097366473
dc.identifier.scopusqualityQ1
dc.identifier.startpage4429
dc.identifier.urihttps://doi.org/10.1080/07391102.2020.1857842
dc.identifier.urihttps://hdl.handle.net/11772/22889
dc.identifier.volume40
dc.identifier.wosWOS:000597030900001
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTaylor & Francis Inc
dc.relation.ispartofJournal of Biomolecular Structure & Dynamics
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.relation.sdgGoal-03: Good Health and Well-Being
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzWoS_20251016
dc.subjectPhthalocyanine
dc.subjectTriazole
dc.subjectEnzyme Inhibition
dc.subjectMolecular Docking
dc.subjectDft Studies
dc.title1,2,3-Triazole substituted phthalocyanine metal complexes as potential inhibitors for anticholinesterase and antidiabetic enzymes with molecular docking studies
dc.typeArticle
dspace.entity.typePublication
relation.isAuthorOfPublicationdadfa319-65b8-4543-92b4-bea49e0139e9
relation.isAuthorOfPublication.latestForDiscoverydadfa319-65b8-4543-92b4-bea49e0139e9

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