1,2,3-Triazole substituted phthalocyanine metal complexes as potential inhibitors for anticholinesterase and antidiabetic enzymes with molecular docking studies
| Autor: | Umit M. Kocyigit, Hasan Yakan, Parham Taslimi, Emre Güzel, Halit Muğlu, Burak Tüzün |
|---|---|
| Přispěvatelé: | Sivas Meslek Yüksekokulu, Eczacılık Fakültesi |
| Rok vydání: | 2022 |
| Předmět: |
animal structures
1 2 3-Triazole Indoles Glycoside Hydrolases 030303 biophysics Triazole Isoindoles Metal 03 medical and health sciences chemistry.chemical_compound Structure-Activity Relationship DFT studies Structural Biology Coordination Complexes Hypoglycemic Agents molecular docking enzyme inhibition Molecular Biology Phthalocyanin etriazole enzyme inhibition molecular docking DFT studies chemistry.chemical_classification 0303 health sciences integumentary system Phthalocyanine General Medicine Triazoles Acetylcholinesterase Combinatorial chemistry Molecular Docking Simulation Enzyme inhibition triazole Enzyme chemistry visual_art visual_art.visual_art_medium Cholinesterase Inhibitors |
| Zdroj: | JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS |
| Popis: | In recent years, acetylcholinesterase (AChE) and α-glycosidase (α-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 Ki values in the range of 40.11 ± 5.61 to 78.27 ± 15.42 µM. For α-glycosidase, the most effective Ki values of compounds 1 and 2 were with Ki values of 16.11 ± 3.13 and 18.31 ± 2.42 µM, 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 α-glycosidase for ID 1R47 (α-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. Communicated by Ramaswamy H. Sarma |
| Databáze: | OpenAIRE |
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