The palladium-based complexes bearing 1,3-dibenzylbenzimidazolium with morpholine, triphenylphosphine, and pyridine derivate ligands: synthesis, characterization, structure and enzyme inhibitions

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AKTAŞ A., Yakalı G., Demir Y., GÜLÇİN İ., AYGÜN M., GÖK Y.

Heliyon, cilt.8, sa.9, 2022 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 8 Sayı: 9
  • Basım Tarihi: 2022
  • Doi Numarası: 10.1016/j.heliyon.2022.e10625
  • Dergi Adı: Heliyon
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, CAB Abstracts, Food Science & Technology Abstracts, Veterinary Science Database, Directory of Open Access Journals
  • Anahtar Kelimeler: Acetylcholinesterase, Bio-catalysis, NHC, Palladium complexes, PEPPSI, Single crystal, Carbonic anhydrases, HETEROCYCLIC CARBENE COMPLEXES, CARBONIC-ANHYDRASE I, CRYSTAL-STRUCTURE, COORDINATION CHEMISTRY, BIOLOGICAL EVALUATION, ANTITUMOR-ACTIVITY, ALPHA-GLYCOSIDASE, HCA I, ACETYLCHOLINESTERASE, BUTYRYLCHOLINESTERASE
  • Atatürk Üniversitesi Adresli: Evet

Özet

© 2022The palladium-based complexes bearing N-heterocyclic carbene (NHC) ligand have long attracted attention as active catalysts for many catalytic reactions. Recently, the biological activities of these complexes, which are stable to air and moisture, have also been wondered. With the aim, we report the synthesis of a series of (NHC)Pd(Br2)(L) complexes (NHC: 1,3-dibenzylbenzimidazolium, L: morpholine, triphenylphosphine, pyridine, 3-chloropyridine, and 2-aminopyridine). All complexes were characterized by NMR (1H and 13C), FTIR spectroscopic and elemental analysis techniques. In addition, the single crystal structures of the complex 3, 4, and 6 were determined through single crystal x-ray crystallographic method. Furthermore, the carbonic anhydrase I and II isoenzymes (hCAs) and acetylcholinesterase (AChE) inhibition effects of these palladium-based complexes bearing NHC ligand were investigated. They showed highly potent inhibition effect with Ki values are between 10.06 ± 1.49–68.56 ± 11.53 nM for hCA I isoenzyme, 7.74 ± 0.66 to 49.39 ± 6.50 nM for hCA II isoenzyme and 22.83 ± 3.21 to 64.09 ± 9.05 nM for AChE enzyme.