Synthesis of new cyclic thioureas and evaluation of their metal-chelating activity, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibition profiles

TASLIMI P., SUJAYEV A., Garibov E., Nazarov N., Huyut Z., ALWASEL S. H., ...Daha Fazla

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, cilt.31, sa.7, 2017 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 7
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1002/jbt.21897
  • Dergi Adı: JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: acetylcholinesterase, butyrylcholinesterase, carbonic anhydrase, metal chelating, thiourea, ERYTHROCYTES IN-VITRO, LYOPHILIZED AQUEOUS EXTRACT, ISOENZYMES HCA I, ANTIOXIDANT ACTIVITY, POLYPHENOL CONTENTS, ENZYME-ACTIVITY, DERIVATIVES, LACTOPEROXIDASE, PURIFICATION, AVERMECTINS
  • Atatürk Üniversitesi Adresli: Evet

Özet

In the presence of trifluoracetic acid (TFAA), an efficient method for the synthesis of tetra(hexa)hydropyrimidinethione-carboxylates has been used on the basis of three-component condensation of thiourea with its different aldehydes and -diketones. Some novel cyclic thioureas were synthesized, and their hCA I, hCA II, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) inhibitors and metal-chelating properties were evaluated. K-i values of novel synthesized compounds for AChE and BChE are in the range of 51.84-135.96 and 143.96-274.55 nM, respectively. Also, HCA I and II were effectively inhibited by these novel compounds, with K-i values in the range of 404.16-745.13 nM for hCA I and of 434.20-689.57 nM for hCA II, respectively. Additionally, acetazolamide (AZA), clinically used as a CA inhibitor, with a K-i value of 883.68 +/- 121.27 nM in hCA I and 1008.66 +/- 144.70 nM in hCA II. Also, tacrine inhibited AChE and BChE showed K-i values of 314.63 +/- 31.66 and 373.57 +/- 75.07 nM, respectively.