Biologically active phthalocyanine metal complexes: Preparation, evaluation of α‐glycosidase and anticholinesterase enzyme inhibition activities, and molecular docking studies
Citation
Güzel, E., Koçyiğit, Ü. M., Taslimi, P., Erkan, S., & Taskin, O. S. (2021). Biologically active phthalocyanine metal complexes: Preparation, evaluation of α‐glycosidase and anticholinesterase enzyme inhibition activities, and molecular docking studies. Journal of Biochemical and Molecular Toxicology, 35(6), 1-9.Abstract
In this study, preparation, as well as investigation of α‐glycosidase and cholinesterase
(ChE) enzyme inhibition activities of furan‐2‐ylmethoxy‐substituted compounds
1–7, are reported. Peripherally, tetra‐substituted copper and manganese
phthalocyanines (5 and 6) were synthesized for the first time. The substitution of
furan‐2‐ylmethoxy groups provides remarkable solubility to the complex and redshift
of the phthalocyanines Q‐band. Besides, the inhibitory effects of these compounds
on acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and
α‐glycosidase (α‐Gly) enzymes have been investigated. The AChE was inhibited by
these compounds (1–7) in low micromolar levels, and Ki values were recorded
between 11.17 ± 1.03 and 83.28 ± 11.08 μM. Against the BChE, the compounds
demonstrated Ki values from 7.55 ± 0.98 to 81.35 ± 12.80 μM. Also, these compounds
(1–7) effectively inhibited α‐glycosidase, with Ki values in the range of
744.87 ± 67.33 to 1094.38 ± 88.91 μM. For α‐glycosidase, the most effective Ki
values of phthalocyanines 3 and 6 were with Ki values of 744.87 ± 67.33 and
880.36 ± 56.77 μM, respectively. Moreover, the studied metal complexes were
docked with target proteins PDB ID: 4PQE, 1P0I, and 3WY1. Pharmacokinetic
parameters and secondary chemical interactions that play an active role in interaction
were predicted with docking simulation results. Overall, furan‐2‐ylmethoxysubstituted
phthalocyanines can be considered as potential agents for the treatment
of Alzheimer's diseases and diabetes mellitus.
Source
Journal of Biochemical and Molecular ToxicologyVolume
35Issue
6URI
https://onlinelibrary.wiley.com/doi/full/10.1002/jbt.22765https://hdl.handle.net/20.500.12418/14853