In Vitro and In Silico DNA Interaction and α-Glucosidase Inhibition Studies of Two Water-Soluble Copper(II) and Cobalt(II) Phthalocyanine Complexes


Yazici F., YILDIRIM AKATIN M., Cesme M., BIYIKLIOĞLU Z., İNAN BEKTAŞ K., SAĞLAM ERTUNGA N.

CHEMISTRYSELECT, cilt.11, sa.11, 2026 (SCI-Expanded, Scopus) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 11 Sayı: 11
  • Basım Tarihi: 2026
  • Doi Numarası: 10.1002/slct.202506405
  • Dergi Adı: CHEMISTRYSELECT
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Chemical Abstracts Core
  • Karadeniz Teknik Üniversitesi Adresli: Evet

Özet

In this study, we evaluated the DNA interactions and antidiabetic activities of two water-soluble, peripherally tetra-({6-[3-(dimethylamino)phenoxy]hexyl}oxy) substituted phthalocyanine complexes (CuPc and CoPc) using combined in vitro and in silico approaches. DNA interactions were investigated by electronic absorption titrations, melting temperature (T m) analysis, and agarose gel electrophoresis. The spectroscopic results indicated that CuPc and CoPc effectively bind to CT-DNA with binding constants (K b) of 1.0 & times; 105 M-1 and 2.0 & times; 105 M-1, respectively, and interact with CT-DNA via a noncovalent binding mode. These complexes also exhibited notable cleavage activities on pBR322 plasmid DNA. Docking analyses indicated preferential binding in the DNA major groove via electrostatic forces, hydrogen bonding, and hydrophobic effects. alpha-Glucosidase inhibition assays showed that the complexes were similar to 1000-fold more effective inhibitors than acarbose, and CuPc inhibited the enzyme in a noncompetitive manner. Docking against alpha-glucosidase yielded binding scores of -9.3 and -9.4 kcal/mol for CuPc and CoPc, respectively, in agreement with the experimental results. In summary, these findings identify CuPc and CoPc as promising phthalocyanine complexes, supported by consistent experimental and computational evidence of DNA interaction and potent alpha-glucosidase inhibition.