Bioactivity and molecular docking studies of some nickel complexes: New analogues for the treatment of Alzheimer, glaucoma and epileptic diseases

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dc.authoridSEN, FATIH/0000-0001-9929-9556
dc.authoridTaslimi, Parham/0000-0002-3171-0633
dc.authoridKorkmaz, Nesrin/0000-0002-7896-1042
dc.authoridKaradag, Ahmet/0000-0003-4676-683X
dc.authoridTUZUN, BURAK/0000-0002-0420-2043
dc.contributor.authorKisa, Dursun
dc.contributor.authorKorkmaz, Nesrin
dc.contributor.authorTaslimi, Parham
dc.contributor.authorTuzun, Burak
dc.contributor.authorTekin, Saban
dc.contributor.authorKaradag, Ahmet
dc.contributor.authorSen, Fatih
dc.date.accessioned2024-10-26T18:11:03Z
dc.date.available2024-10-26T18:11:03Z
dc.date.issued2020
dc.departmentSivas Cumhuriyet Üniversitesi
dc.description.abstractThe interaction of the coordination compounds with biological molecules resulted in the investigation of the drug potential of these molecules. In this study, enzyme inhibition of DSA (1-3) coordination compounds that were previously investigated for their anticancer and antibacterial properties was investigated. Also, DSA (1-3) had Ki values of 635.30 + 152.62, 184.01 + 90.05, and 163.03 +/- 60.01 mu M against human carbonic anhydrase I, 352.23 +/- 143.09, 46.2 +/- 15.47, and 54.117 +/- 18.80 mu M against AChE, 310.64 +/- 97.35, 35.54 +/- 7.01, and 101.51 +/- 15.314 mu M against BChE, respectively. The biological activity values of these compounds against enzymes whose name are AChE, BChE, and hCAI were compared. Ellman and Verporte methods were used for the study of these enzymes. Cholinesterase inhibitors, also known as anti-cholinesterase and cholinesterase blocking drugs, are chemicals that prevent the breakdown of the neurotransmitter acetylcholine or butyr-ylcholine. They may be used as drugs for Alzheimer's and myasthenia gravis. It is a common method for com-paring biological activity values of nickel complexes with molecular docking calculations. Nickel complexes were studied against enzymes that are human carbonic anhydrase isozyme I for ID 2CAB (hCA I), butyr-ylcholinesterase for ID 1P0I (BChE), and acetylcholinesterase for ID 1EEA (AChE), respectively.
dc.description.sponsorshipScientific Research Projects Commission, Bartin University, Bartin -TURKEY [2019-FEN-B-001]
dc.description.sponsorshipThis work is supported by the Scientific Research Projects Commission, Bartin University, Bartin -TURKEY (Grand ID/Project No: 2019-FEN-B-001).
dc.identifier.doi10.1016/j.bioorg.2020.104066
dc.identifier.issn0045-2068
dc.identifier.issn1090-2120
dc.identifier.pmid32650180
dc.identifier.scopus2-s2.0-85087409137
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.bioorg.2020.104066
dc.identifier.urihttps://hdl.handle.net/20.500.12418/30475
dc.identifier.volume101
dc.identifier.wosWOS:000552631100008
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherAcademic Press Inc Elsevier Science
dc.relation.ispartofBioorganic Chemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectNickel complexes
dc.subjectEnzyme inhibition
dc.subjectMetabolic enzymes
dc.subjectMolecular docking
dc.titleBioactivity and molecular docking studies of some nickel complexes: New analogues for the treatment of Alzheimer, glaucoma and epileptic diseases
dc.typeArticle

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