Design, synthesis, and enzyme inhibition evaluation of some novel Mono- and Di-O-β-D-Glycopyranosyl Chalcone analogues with molecular docking studies

Celik G., TATAR YILMAZ G., Sahin H., BARUT B., YAYLI N.

TURKISH JOURNAL OF CHEMISTRY, cilt.47, sa.1, ss.171-184, 2023 (SCI-Expanded) identifier identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 47 Sayı: 1
  • Basım Tarihi: 2023
  • Doi Numarası: 10.55730/1300-0527.3527
  • Dergi Adı: TURKISH JOURNAL OF CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chemical Abstracts Core, TR DİZİN (ULAKBİM)
  • Sayfa Sayıları: ss.171-184
  • Karadeniz Teknik Üniversitesi Adresli: Evet

Özet

In this study, some novel mono-and di-O-beta-D-glycopyranosyl chalcone analogs were designed, synthesized, and characterized. The chalcone derivatives were synthesized with good yields by base-catalyzed Claisen-Schmidt condensation in EtOH solution. Then these chalcones were reacted with TAGBr (2,3,4,6-tetra-O-acetyl-alpha-D-glucopyranosylbromide) in dry acetone under the anhydrous condition at 0-5 degrees C. Deacylated was carried out by the Zemplen's method with NaOCH3 in dry methanol results in substituted chalcone-O-glycosides (mono-and di-O-beta-D-glycopyranosyl chalcone analogs). The chemical structures of all synthesized compounds were elucidated based on IR, NMR spectral data, and mass spectrometry. Further, the compounds (7a-c, 8a-c, 12a-c, 16a-c, and 17a-c) were tested for their enzyme inhibition activity against alpha-glycosidase, tyrosinase, and AChE with in vitro and in silico analysis. Amongst them, compounds 12a-c, 16a-c, and 17a-c displayed moderate or less enzyme inhibition activity against alpha-glycosidase while other compounds 7a-c and 8a-c) were not active. Remarkably interesting enzyme inhibition effects, with IC50 values below 30.59 +/- 0.30 mu M were recorded with 7c (IC50=11.07 +/- 0.55 mu M) against tyrosinase.