Phthalocyanine complexes with (4-isopropylbenzyl)oxy substituents: preparation and evaluation of anti-carbonic anhydrase, anticholinesterase enzymes and molecular docking studies

Abstract

In this study, the preparation, aggregation behavior and investigation of carbonic anhydrase and cholinesterase enzyme inhibition features of non-peripherally (4-isopropylbenzyl)oxy-substituted phthalocyanines (4–6) are reported for the first time. The chemical structures of these new phthalocyanines were elucidated by UV-Vis (ultraviolet-visible), FT-IR (Fourier transform infrared spectrometry), NMR (nuclear magnetic resonance) and MALDI-TOF (matrix-assisted laser desorption/ionization time-of-flight) mass spectrometry. The substitution of 4-isopropylbenzyl)oxy groups benefits a remarkable solubility and redshift of the phthalocyanines Q-band. Also, these complexes were tested against some enzymes such as butyrylcholinesterase enzyme, human carbonic anhydrase I and II isoforms and acetylcholinesterase enzyme. The phthalocyanine complexes showed Ki values of in the range of 478.13 ± 57.25–887.25 ± 101.20 µM against hCA I, 525.16 ± 45.87–921.14 ± 81.25 µM against hCA II, 68.33 ± 9.13–201.15 ± 35.86 µM against AChE and 86.25 ± 13.65–237.54 ± 24.7 µM against BChE. Molecular docking studies were performed to investigate the binding modes and interaction energies of the (2–6) complexes with the hCA I (PDB ID:1BMZ), hCA II (PDB ID:2ABE), AChE (PDB ID:4EY6) and BChE (PDB ID:2PM8).

Graphical Abstract

Communicated by Ramaswamy H. Sarma

Keywords:

• Phthalocyanine
• carbonic anhydrase
• cholinesterase
• enzyme inhibition
• molecular docking

Disclosure statement

The authors declare that there is no conflict of interest.

Additional information

Funding

This work was supported by the Research Fund of the Sakarya University (Project No: 2019-5-19-174) and Sakarya University of Applied Sciences.