Synthesis of zinc phthalocyanine containing 1,2-phenylene bis(3-chloropropanoate) substituted groups and investigation of their metabolic enzyme inhibitory effects

Güngördü Solğun D., Sadeghian N., Taslimi P., Taskin-Tok T., Ağırtaş M. S.

Polyhedron, cilt.264, 2024 (SCI-Expanded) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 264
  • Basım Tarihi: 2024
  • Doi Numarası: 10.1016/j.poly.2024.117251
  • Dergi Adı: Polyhedron
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chemical Abstracts Core, Chimica
  • Anahtar Kelimeler: Enzyme inhibition, Fluorescence, Molecular docking, Phthalocyanine, Synthesis
  • Van Yüzüncü Yıl Üniversitesi Adresli: Evet

Özet

In this study, 4,5-dicyano-1,2-phenylene dinicotinate compound was obtained as a result of the reaction of 4,5-dichlorophthalonitrile and nicotinic acid. This compound was reacted with the zinc chloride salt to obtain the original zinc phthalocyanine compound bearing 1,2-phenylene bis(3-chloropropanoate) substituted groups. This compound and its starting material were characterized with the assist of 1H NMR, IR, UV–vis, Mass spectrum. In the docking study of compounds (3) and (4) against each target (AChE, BChE, α-Amy and α-Gly), Zn complex (4) exhibits more binding affinity with the target models considered compared to ligand structure (3). Especially, AChE protein and complex (4) form the best binding affinity with a binding energy value of −10.55 kcal/mol. They are compatible and supportive with the data obtained as a result of in vitro analysis. These 4,5-dicyano-1,2-phenylene dinicotinate (3) and 2, 10, 16, 24 – tetrakis 1,2-phenylene bis(3-chloropropanoate) phthalocyaninato) zinc(II) (4) complexes had effective inhibition against α-glucosidase, α-amylase, butyrylcholinesterase and AChE. Also, IC50 amounts were found as 7.84 and 12.36 µM for AChE, 3.80 and 4.56 µM for BChE, 27.08 and 38.14 µM for α-amylase, and 5.30 and 9.73 µM for α-glucosidase.