Synthesis, characterization and bioactivities of dative donor ligand N-heterocyclic carbene (NHC) precursors and their Ag(I)NHC coordination compounds

Kazancı A., GÖK Y., Kaya R., AKTAŞ A., Taslimi P., GÜLÇİN İ.

Polyhedron, cilt.193, 2021 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 193
  • Basım Tarihi: 2021
  • Doi Numarası: 10.1016/j.poly.2020.114866
  • Dergi Adı: Polyhedron
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chemical Abstracts Core
  • Anahtar Kelimeler: Dative donor ligand, Enzyme inhibition, Carbonic anhydrase, N-phthalimidomethyl, Silver(I)NHC complex, ANHYDRASE INHIBITORY PROPERTIES, PEPPSI COMPLEXES SYNTHESIS, BIS-BENZIMIDAZOLIUM SALTS, POTENT CARBONIC-ANHYDRASE, ERYTHROCYTES IN-VITRO, CRYSTAL-STRUCTURE, CATALYTIC-ACTIVITY, II INHIBITION, ISOENZYMES I, HCA I
  • Atatürk Üniversitesi Adresli: Evet

Özet

© 2020 Elsevier LtdThis study contains the synthesis of N-phthalimidomethyl-substituted NHC precursors and their Ag(I)NHC coordination compounds. The NHC precursors were synthesized from the 1-(N-phthalimidomethyl)benzimidazole and alkyl/aryl halide. The Ag(I)NHC coordination compounds were synthesized from the N-phthalimidomethyl substituted benzimidazolium salts and silver oxide via the in-situ deprotonation method. The formation of all compounds was proved fully by 1H NMR, 13C NMR, FTIR and elemental analysis techniques. Also, these novel N-phthalimidomethyl substituted NHC precursors and Ag(I)NHC coordination compounds were found as effective inhibitors for acetylcholinesterase (AChE), human carbonic anhydrase I isoenzyme (hCA I), human carbonic anhydrase II isoenzyme (hCA II), and butyrylcholinesterase (BChE) with inhibition constants (Kis) in the range of 1.00 ± 0.14–2.31 ± 0.58 µM for hCA I, 1.30 ± 0.21–2.85 ± 0.56 µM for hCA II, 0.35 ± 0.06–2.58 ± 0.70 µM for AChE, and 0.42 ± 0.01–1.27 ± 0.16 µM for BChE, respectively.