Synthesis of new cyclic thioureas and evaluation of their metal-chelating activity, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibition profiles
JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, cilt.31, sa.7, 2017 (SCI-Expanded, Scopus)
- 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.