Synthesis, characterization, DNA interaction, molecular docking, α-amylase and α-glucosidase inhibition studies of a water soluble Zn(II) phthalocyanine

Sağlam Ertunga N., Saka E. T., Taşkın T., İnan Bektaş K., Yıldırım Akatın M.

DALTON TRANSACTIONS, cilt.1, sa.1, ss.1-10, 2024 (SCI-Expanded)

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 1 Sayı: 1
  • Basım Tarihi: 2024
  • Doi Numarası: 10.1039/d4dt01138d
  • Dergi Adı: DALTON TRANSACTIONS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Applied Science & Technology Source, Aquatic Science & Fisheries Abstracts (ASFA), Chemical Abstracts Core, Chimica, Communication Abstracts, Compendex, EMBASE, MEDLINE
  • Sayfa Sayıları: ss.1-10
  • Karadeniz Teknik Üniversitesi Adresli: Evet

Özet

In this study, 2(3), 9(10), 16(17), 23(24)-Tetrakis-[N-methyl-(1-benzylpiperidin-4-yl)oxy)phthalocyaninato]zinc(II) iodide (ZnPc-2) was synthesized and characterized with spectral methods (FT-IR, 1H-NMR, UV-Vis and mass). The interaction of ZnPc-2 with DNA was investigated by using UV/Vis titrimetric method, thermal denaturation profile, agarose gel electrophoresis and molecular docking studies. Additionally, the antidiabetic activity of ZnPc-2 was revealed spectroscopically by studying α-amylase and α-glucosidase inhibition activities. The spectroscopic results indicated that ZnPc-2 effectively binds to calf thymus-DNA (CT-DNA) with a Kb value of 7.5x104 M-1 and interacts with CT-DNA via noncovalent binding mode. Gel electrophoresis results also show that ZnPc-2 binds strongly to DNA molecules and exhibits effective nuclease activity even at low concentrations. Furthermore, docking studies suggest that ZnPc-2 exhibits a stronger binding tendency with DNA than the control compounds ethidium bromide and cisplatin. Consequently, due to its strong DNA binding and nuclease activity, ZnPc-2 may be suitable for antimicrobial and anticancer applications after further toxicological test systems. Additionally, antidiabetic studies showed that ZnPc-2 had both α-amylase and α-glucosidase inhibition activity. Moreover, the α-glucosidase inhibitory effect of ZnPc-2 was approximately 3500 times higher than the standard inhibitor acarbose. Considering this results, it can be said that ZnPc-2 is a moderate α-amylase and a highly effective α-glucosidase inhibitor. This suggests that ZnPc-2 may have the potential to be used as a therapeutic agent for the treatment of type 2 diabetes.