Design, synthesis, characterization, crystal structure, in silico studies, and inhibitory properties of the PEPPSI type Pd(II)NHC complexes bearing chloro/fluorobenzyl group

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dc.authoridGulcin, ilhami/0000-0001-5993-1668
dc.authoridAygün, Muhittin/0000-0001-9670-9062
dc.authoridAktaş, Aydın/0000-0001-8496-6782
dc.authoridTaslimi, Parham/0000-0002-3171-0633
dc.authorwosidTaslimi, Parham/AAL-2788-2020
dc.authorwosidGulcin, ilhami/F-1428-2014
dc.authorwosidAygün, Muhittin/E-9590-2011
dc.authorwosidAktaş, Aydın/J-6194-2019
dc.contributor.authorGok, Yetkin
dc.contributor.authorTaslimi, Parham
dc.contributor.authorSen, Betul
dc.contributor.authorBal, Selma
dc.contributor.authorAktas, Aydin
dc.contributor.authorAygun, Muhittin
dc.contributor.authorSadeghi, Morteza
dc.date.accessioned2024-08-04T20:53:35Z
dc.date.available2024-08-04T20:53:35Z
dc.date.issued2023
dc.departmentİnönü Üniversitesien_US
dc.description.abstractThis work contains synthesis, characterization, crystal structure, and biological activity of a new series of the PEPPSI type Pd(II)NHC complexes [(NHC)Pd(II)(3-Cl-py)]. NMR, FTIR, and elemental analysis techniques were used to characterize all (NHC)Pd(II)(3-Cl-py) complexes. Also, molecular and crystal structures of complex 1c were established by single-crystal X-ray diffraction. Regarding the X-ray studies, the palladium(II) atom has a slightly distorted square-planar coordination environment. Additionally, the enzyme inhibitory effect of new (NHC)Pd(II)(3-Cl-py) complexes (1a-1g) was studied. They exhibited highly potent inhibition effect on acetyl -cholinesterase (AChE), butyrylcholinesterase (BChE) and carbonic anhydrases (hCAs) (Ki values are in the range of 0.08 +/- 0.01 to 0.65 +/- 0.06 mu M, 10.43 +/- 0.98 to 22.48 +/- 2.01 mu M, 6.58 +/- 0.30 to 10.88 +/- 1.01 mu M and 6.34 +/- 0.37 to 9.02 +/- 0.72 mu M for AChE, BChE, hCA I, and hCA II, respectively). Based on the molecular docking, among the seven synthesized complexes, 1c, 1b, 1e, and 1a significantly inhibited AChE, BChE, hCA I, and hCA II enzymes, respectively. The findings highpoint that (NHC)Pd(II)(3-Cl-py) complexes can be considered as possible inhibitors via metabolic enzyme inhibition.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 characterization of compounds. Dokuz Eylul University for the use of the Oxford Rigaku Xcalibur Eos Diffractometer (purchased under University Research Grant No: 2010.KB.FEN.13) is also greatly acknowledged.en_US
dc.identifier.doi10.1016/j.bioorg.2023.106513
dc.identifier.issn0045-2068
dc.identifier.issn1090-2120
dc.identifier.pmid37030104en_US
dc.identifier.scopus2-s2.0-85151625865en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://doi.org/10.1016/j.bioorg.2023.106513
dc.identifier.urihttps://hdl.handle.net/11616/101273
dc.identifier.volume135en_US
dc.identifier.wosWOS:000978114900001en_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.subjectSynthesisen_US
dc.subjectEnzyme inhibitionen_US
dc.subjectButyrylcholinesteraseen_US
dc.subjectNHCen_US
dc.subjectPEPPSIen_US
dc.subjectMolecular dockingen_US
dc.subjectX-ray diffractionen_US
dc.titleDesign, synthesis, characterization, crystal structure, in silico studies, and inhibitory properties of the PEPPSI type Pd(II)NHC complexes bearing chloro/fluorobenzyl groupen_US
dc.typeArticleen_US

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