Synthesis of<i> N</i>-substituted 4-phenyl-2-aminothiazole derivatives and investigation of their inhibition properties against<i> h</i>CA I, II, and AChE enzymes

BİÇER A., ÇAĞLAYAN C., DEMİR Y., Turkes C., ALTUNDAŞ R., Akyildiz H., ...Daha Fazla

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, cilt.761, 2024 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 761
  • Basım Tarihi: 2024
  • Doi Numarası: 10.1016/j.abb.2024.110159
  • Dergi Adı: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Chemical Abstracts Core, EMBASE, Food Science & Technology Abstracts, MEDLINE, Veterinary Science Database
  • Anadolu Üniversitesi Adresli: Evet

Özet

In this study, thiazole derivatives containing sulphonamide, amide, and phenyl amino groups were synthesized to protect the free amino groups of 5-methyl-4-phenyl-2-aminothiazole and 4-phenyl-2-aminothiazole. Halogenated reactions of N-protected thiazole derivatives have been investigated. LCMS, FT-IR, 1 H NMR, and 13 C NMR spectroscopy techniques were used to elucidate the structures of the synthesized compounds. Inhibition effects of the N-protected thiazole derivatives against human carbonic anhydrase I, II (hCA h CA I, h CA II), and acetylcholinesterase (AChE) were investigated. The best results among the synthesized N-protected thiazole derivatives showed Ki i values in the range of 46.85-587.53 nM against h CA I, 35.01-578.06 nM against h CA II, and in the range of 19.58-226.18 nM against AChE. Furthermore, in silico studies with the target enzyme of the thiazole derivatives (9 and 11), , which showed the best results experimentally, have examined the binding interactions of the related compounds at the enzyme active site.