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

dc.contributor.authorKoçyiğit, Ümit M.
dc.contributor.authorTaslimi, Parham
dc.contributor.authorTüzün, Burak
dc.contributor.authorYakan, Hasan
dc.contributor.authorMuğlu, Halit
dc.contributor.authorGüzel, Emre
dc.date.accessioned2026-01-04T14:44:59Z
dc.date.issued2020-12-09
dc.description.abstractIn 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.urihttps://doi.org/10.1080/07391102.2020.1857842
dc.description.urihttps://dx.doi.org/10.6084/m9.figshare.13352420.v1
dc.description.urihttps://dx.doi.org/10.6084/m9.figshare.13352420
dc.description.urihttps://pubmed.ncbi.nlm.nih.gov/33292060
dc.description.urihttps://dx.doi.org/10.1080/07391102.2020.1857842
dc.description.urihttps://hdl.handle.net/20.500.14002/388
dc.description.urihttps://hdl.handle.net/20.500.12418/13861
dc.description.urihttps://hdl.handle.net/20.500.12418/13570
dc.description.urihttp://hdl.handle.net/11772/11643
dc.description.urihttps://hdl.handle.net/11772/22889
dc.description.urihttp://hdl.handle.net/11772/9329
dc.description.urihttps://aperta.ulakbim.gov.tr/record/10181
dc.description.urihttps://doi.org/https://doi.org/20.500.12418/13861
dc.description.urihttps://doi.org/https://doi.org/10.1080/07391102.2020.1857842
dc.description.urihttps://doi.org/https://doi.org/20.500.12418/13570
dc.identifier.doi10.1080/07391102.2020.1857842
dc.identifier.eissn1538-0254
dc.identifier.endpage4439
dc.identifier.issn0739-1102
dc.identifier.openairedoi_dedup___::fd9b988a0aae91a813521252a713ee7c
dc.identifier.orcid0000-0001-8710-2912
dc.identifier.orcid0000-0002-3171-0633
dc.identifier.orcid0000-0002-0420-2043
dc.identifier.orcid0000-0002-1142-3936
dc.identifier.pubmed33292060
dc.identifier.scopus2-s2.0-85097366473
dc.identifier.startpage4429
dc.identifier.urihttps://hdl.handle.net/20.500.12597/38389
dc.identifier.volume40
dc.identifier.wos000597030900001
dc.language.isoeng
dc.publisherInforma UK Limited
dc.relation.ispartofJournal of Biomolecular Structure and Dynamics
dc.rightsOPEN
dc.subjectIndoles
dc.subjectEnzyme Inhibition
dc.subjectGlycoside Hydrolases
dc.subjectDft Studies
dc.subjectIsoindoles
dc.subjectStructure-Activity Relationship
dc.subjectDFT studies
dc.subjectCoordination Complexes
dc.subjectHypoglycemic Agents
dc.subjectmolecular docking
dc.subjectMolecular Biology
dc.subjectenzyme inhibition
dc.subjectPhthalocyanin etriazole enzyme inhibition molecular docking DFT studies
dc.subjectPhthalocyanine
dc.subjectmolecular docking
dc.subjectTriazoles
dc.subjectMolecular Docking
dc.subjectMolecular Docking Simulation
dc.subjecttriazole
dc.subjectAcetylcholinesterase
dc.subjectTriazole
dc.subjectCholinesterase Inhibitors
dc.subject.sdg3. Good health
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
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