1,2,3-Triazole substituted phthalocyanine metal complexes as potential inhibitors for anticholinesterase and antidiabetic enzymes with molecular docking studies

Creative Commons License

KOÇYİĞİT Ü. M., Taslimi P., TÜZÜN B., Yakan H., MUĞLU H., Guzel E.

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, vol.40, no.10, pp.4429-4439, 2022 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 40 Issue: 10
  • Publication Date: 2022
  • Doi Number: 10.1080/07391102.2020.1857842
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, CAB Abstracts, Chemical Abstracts Core, EMBASE, MEDLINE
  • Page Numbers: pp.4429-4439
  • Keywords: Phthalocyanine, triazole, enzyme inhibition, molecular docking, DFT studies
  • Ondokuz Mayıs University Affiliated: Yes


In recent years, acetylcholinesterase (AChE) and alpha-glycosidase (alpha-gly) inhibition have emerged as a promising and important approach for pharmacological intervention in many diseases such as glaucoma, epilepsy, obesity, cancer, and Alzheimer's. In this manner, the preparation and enzyme inhibition activities of peripherally 1,2,3-triazole group substituted metallophthalocyanine derivatives with strong absorption in the visible region were presented. These novel metallophthalocyanine derivatives (2-6) effectively inhibited AChE, with K-i values in the range of 40.11 +/- 5.61 to 78.27 +/- 15.42 mu M. For alpha-glycosidase, the most effective K-i values of compounds 1 and 2 were with K-i values of 16.11 +/- 3.13 and 18.31 +/- 2.42 mu M, respectively. Also, theoretical calculations were investigated to compare the chemical and biological activities of the ligand (1) and its metal complexes (2-6). Biological activities of 1 and its complexes against acetylcholinesterase for ID 4M0E (AChE) and alpha-glycosidase for ID 1R47 (alpha-gly) are calculated. Theoretical calculations were compatible with the experimental results and these 1,2,3-triazole substituted phthalocyanine metal complexes were found to be efficient inhibitors for anticholinesterase and antidiabetic enzymes.