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

Guzel E., KOÇYİĞİT Ü. M., Taslimi P., GÜLÇİN İ., ERKAN S., NEBİOĞLU M., ...Daha Fazla

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, cilt.40, sa.2, ss.733-741, 2022 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 40 Sayı: 2
  • Basım Tarihi: 2022
  • Doi Numarası: 10.1080/07391102.2020.1818623
  • Dergi Adı: JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, Chemical Abstracts Core, EMBASE, MEDLINE
  • Sayfa Sayıları: ss.733-741
  • Anahtar Kelimeler: Phthalocyanine, carbonic anhydrase, cholinesterase, enzyme inhibition, molecular docking, SILICON IV PHTHALOCYANINES, PHOTODYNAMIC INACTIVATION, METAL-COMPLEXES, ZINC, ELECTROCHEMISTRY, DERIVATIVES, INHIBITORS, ACID
  • Sivas Cumhuriyet Üniversitesi Adresli: Evet

Özet

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 mu M against hCA I, 525.16 +/- 45.87-921.14 +/- 81.25 mu M against hCA II, 68.33 +/- 9.13-201.15 +/- 35.86 mu M against AChE and 86.25 +/- 13.65-237.54 +/- 24.7 mu M 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).