Novel 2-aminopyridine liganded Pd(II) N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure and bioactivity properties

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dc.authoridAktaş, Aydın/0000-0001-8496-6782
dc.authoridGulcin, ilhami/0000-0001-5993-1668
dc.authoridsağlamtaş, rüya/0000-0002-4400-2302
dc.authoridDemir, Yeliz/0000-0003-3216-1098
dc.authoridTaslimi, Parham/0000-0002-3171-0633
dc.authorwosidAktaş, Aydın/J-6194-2019
dc.authorwosidGök, Yetkin/AAA-5669-2021
dc.authorwosidGulcin, ilhami/F-1428-2014
dc.authorwosidkaya, rüya/AAB-2401-2021
dc.authorwosidsağlamtaş, rüya/ABC-8186-2021
dc.authorwosidBarut Celepci, Duygu/M-6189-2017
dc.authorwosidTaslimi, Parham/AAL-2788-2020
dc.contributor.authorErdemir, Pato
dc.contributor.authorCelepci, Duygu Barut
dc.contributor.authorAktas, Aydin
dc.contributor.authorGok, Yetkin
dc.contributor.authorKaya, Ruya
dc.contributor.authorTaslimi, Parham
dc.contributor.authorDemir, Yeliz
dc.date.accessioned2024-08-04T20:46:05Z
dc.date.available2024-08-04T20:46:05Z
dc.date.issued2019
dc.departmentİnönü Üniversitesien_US
dc.description.abstractIn this work, the synthesis, crystal structure, characterization, and enzyme inhibition effects of the novel a series of 2-aminopyridine liganded Pd(II) N-heterocyclic carbene (NHC) complexes were examined. These complexes of the Pd-based were synthesized from PEPPSI complexes and 2-aminopyridine. The novel complexes were characterized by using C-13 NMR, H-1 NMR, elemental analysis, and FTIR spectroscopy techniques. Also, crystal structures of the two compounds were recorded by using single-crystal X-ray diffraction assay. Also, these complexes were tested toward some metabolic enzymes like a-glycosidase, aldose reductase, butyrylcholinesterase, acetylcholinesterase enzymes, and carbonic anhydrase I, and II isoforms. The novel 2-aminopyridine liganded (NHC) PdI2(2-aminopyridine) complexes (1a-i) showed Ki values of in range of 5.78 +/- 0.33-22.51 +/- 8.59 nM against hCA I, 13.77 +/- 2.21-30.81 +/- 4.87 nM against hCA II, 0.44 +/- 0.08-1.87 +/- 0.11 nM against AChE and 3.25 +/- 0.34-12.89 +/- 4.77 nM against BChE. Additionally, we studied the inhibition effect of these derivatives on aldose reductase and alpha-glycosidase enzymes. For these compounds, compound 1d showed maximum inhibition effect against AR with a Ki value of 360.37 +/- 55.82 nM. Finally, all compounds were tested for the inhibition of alpha-glycosidase enzyme, which recorded efficient inhibition profiles with Ki values in the range of 4.44 +/- 0.65-12.67 +/- 2.50 nM against aglycosidase.en_US
dc.description.sponsorshipDokuz Eylul University [2010.KB.FEN.13]en_US
dc.description.sponsorshipThe authors thank the Inonu University Faculty of Science Department of Chemistry for the spectroscopy and elemental analysis characterization of compounds and Dokuz Eylul University for the use of the Oxford Rigaku Xcalibur Eos Diffractometer (purchased under University Research Grant No: 2010.KB.FEN.13).en_US
dc.identifier.doi10.1016/j.bioorg.2019.103134
dc.identifier.issn0045-2068
dc.identifier.issn1090-2120
dc.identifier.pmid31374523en_US
dc.identifier.scopus2-s2.0-85069924730en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://doi.org/10.1016/j.bioorg.2019.103134
dc.identifier.urihttps://hdl.handle.net/11616/98889
dc.identifier.volume91en_US
dc.identifier.wosWOS:000487812000032en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherAcademic Press Inc Elsevier Scienceen_US
dc.relation.ispartofBioorganic Chemistryen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectN-heterocyclic carbeneen_US
dc.subject2-aminopyridineen_US
dc.subjectCrystal structureen_US
dc.subjectMetabolic enzymesen_US
dc.subjectEnzyme inhibitionen_US
dc.titleNovel 2-aminopyridine liganded Pd(II) N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure and bioactivity propertiesen_US
dc.typeArticleen_US

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