Inhibition of urease by some new synthesized 1,2,4-triazol derivatives: Inhibition mechanism and molecular docking

KALFA A., DEMIR E., ÇOLAK A., YAŞAR A., BEKİRCAN O.

INDIAN JOURNAL OF CHEMISTRY SECTION B-ORGANIC CHEMISTRY INCLUDING MEDICINAL CHEMISTRY, cilt.58, sa.6, ss.720-726, 2019 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 58 Sayı: 6
  • Basım Tarihi: 2019
  • Dergi Adı: INDIAN JOURNAL OF CHEMISTRY SECTION B-ORGANIC CHEMISTRY INCLUDING MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.720-726
  • Anahtar Kelimeler: Urease, inhibition, triazole, noncompetitive, docking, JACK BEAN UREASE, HELICOBACTER-PYLORI, COMPETITIVE INHIBITORS, IN-VITRO, ANTIFUNGAL, ANTIBACTERIAL, PURIFICATION, SCHIFF, DESIGN
  • Karadeniz Teknik Üniversitesi Adresli: Evet

Özet

Urease is a metalloenzyme that catalyzes the hydrolysis of urea to ammonia and carbon dioxide. This ammonia secretion may cause significant increase in pH and is responsible for negative effects of urease activity in human health and agriculture. So, jack bean urease inhibition potentials of a newly synthesized of 243-(4-chloropheny1)-5-(4-methoxybenzy1)4H-1,2,4-triazol-4-1]acetohydrazide derivative compounds have been investigated in this study. Initially, IC50 values of six molecules (B16-B21) have been determined. According to this, it is seen that the B20 molecule is the most effective inhibitor. Docking studies also supported this end result. Urease inhibition type and K-i value are found to be noncompetitive and 32.01 mu 0.25 mu M, respectively, in the presence of compound B20. These results suggest that the B20 compound is a potential urease inhibitor.