2-Hydroxyethyl substituted NHC precursors: Synthesis, characterization, crystal structure and carbonic anhydrase, alpha-glycosidase, butyrylcholinesterase, and acetylcholinesterase inhibitory properties

Erdemir F., Celepci D. B., AKTAŞ A., TASLIMI P., GÖK Y., Karabiyik H., ...Daha Fazla

JOURNAL OF MOLECULAR STRUCTURE, cilt.1155, ss.797-806, 2018 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 1155
  • Basım Tarihi: 2018
  • Doi Numarası: 10.1016/j.molstruc.2017.11.079
  • Dergi Adı: JOURNAL OF MOLECULAR STRUCTURE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.797-806
  • Anahtar Kelimeler: N-heterocyclic carbenes, Carbonic anhydrase, Cholinesterase, alpha-Glycosidase, X-ray diffraction, HRMS-SPE-NMR, IN-VITRO, ISOENZYMES I, GLUCOSIDASE INHIBITORS, SILVER COMPLEXES, MANNICH-BASES, DERIVATIVES, ANTIOXIDANT, PROFILES, ENZYMES
  • Atatürk Üniversitesi Adresli: Evet

Özet

This study contains novel a serie synthesis of N-heterocyclic carbene (NHC) precursors that 2-hydroxyethyl substituted. The NHC precursors have been prepared from 1-(2-hydroxyethyl)benzimidazole and alkyl halides. The novel NHC precursors have been characterized by using H-1 NMR, C-13 NMR, FTIR spectroscopy and elemental analysis techniques. Molecular and crystal structures of 2a, 2d, 2e, 2f and 2g were obtained with single-crystal X-ray diffraction studies. These novel NHC precursor's derivatives effectively inhibited the a-glycosidase, cytosolic carbonic anhydrase I and II isoforms (hCA I and II), butyrylcholinesterase (BChE) and acetylcholinesterase (AChE). Inhibition constant (K-i) were found in the range of 0.30-9.22 nM for alpha-glycosidase, 13.90-41.46 nM for hCA I, 12.82-49.95 nM for hCA II, 145.82-882.01 nM for BChE, and 280.92-1370.01 nM for AChE, respectively. (C) 2017 Elsevier B.V. All rights reserved.