Synthesis, characterization and crystal structure of 2-(4-hydroxyphenyl)ethyl and 2-(4-nitrophenyl)ethyl Substituted Benzimidazole Bromide Salts: Their inhibitory properties against carbonic anhydrase and acetylcholinesterase

Creative Commons License

Behcet A., Caglilar T., Barut Celepci D., Aktaş A., Taslimi P., Gök Y., ...Daha Fazla

JOURNAL OF MOLECULAR STRUCTURE, cilt.1170, ss.160-169, 2018 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 1170
  • Basım Tarihi: 2018
  • Doi Numarası: 10.1016/j.molstruc.2018.05.077
  • Dergi Adı: JOURNAL OF MOLECULAR STRUCTURE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.160-169
  • Anahtar Kelimeler: N-heterocyclic carbenes precursors, Benzimidazole, Single-crystal X-ray diffraction, Carbonic anhydrase, Acetylcholinesterase, Enzyme inhibition, N-HETEROCYCLIC CARBENES, ISOENZYMES HCA I, COMPLEXES SYNTHESIS, CATALYTIC-ACTIVITY, NHC PRECURSORS, BUTYRYLCHOLINESTERASE, DERIVATIVES, ANTIOXIDANT, ESTERASE, BROMOPHENOLS
  • Dokuz Eylül Üniversitesi Adresli: Evet

Özet

This paper reports the synthesis of 2-(4-hydroxyphenyl)ethyl and 2-(4-nitrophenyl)ethyl substituted benzimidazolium salts. The benzimidazolium salts were synthesized by N-substituted benzimidazolium and aryl halides. The 2-(4-hydroxyphenyl)ethyl and 2-(4-nitrophenyl)ethyl substituted benzimidazolium salts were characterized by using H-1 NMR, C-13 NMR, FT-IR spectroscopy and elemental analysis techniques. Molecular and crystal structure of the complex 2d and 3d were obtained by single-crystal X-ray diffraction method. Additionally, The enzyme inhibition activities of the benzimidazolium salts were investigated. These 2-(4-hydroxyphenyl)ethyl and 2-(4-nitrophenyl)ethyl substituted benzimidazolium salts (1, 2a-g, and 3a-f) showed good inhibitory action against acetylcholinesterase (AChE), and human (h) carbonic anhydrase (CA) isoforms I, and II. Ki values for AChE were in range of 5.97 +/- 0.56 -23.15 +/- 3.98 nM. On the other hand, the hCA I, and II isoenzymes were effectively inhibited by these compounds, with K-i values in the range of 17.33 +/- 4.55-99.23 +/- 44.91 nM for hCA I, and 33.98 +/- 3.43 -113.23 +/- 39.31 nM for hCA II, respectively. (C) 2018 Elsevier B.V. All rights reserved.