dc.contributor.author | Güzel, Emre | |
dc.contributor.author | Koçyiğit, Ümit M. | |
dc.contributor.author | Taslimi, Parham | |
dc.contributor.author | Gülçin, İlhami | |
dc.contributor.author | Erkan, Sultan | |
dc.contributor.author | Nebioğlu, Mehmet | |
dc.contributor.author | Şişman, İlkay | |
dc.date.accessioned | 2022-02-09T12:30:22Z | |
dc.date.available | 2022-02-09T12:30:22Z | |
dc.date.issued | 2020 | |
dc.identifier.issn | 0739-1102 | |
dc.identifier.issn | 1538-0254 | |
dc.identifier.uri | https://doi.org/10.1080/07391102.2020.1818623 | |
dc.identifier.uri | https://hdl.handle.net/20.500.14002/389 | |
dc.description.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 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). | en_US |
dc.description.sponsorship | Research Fund of the Sakarya UniversitySakarya University [2019-5-19-174]; Sakarya University of Applied Sciences | en_US |
dc.description.sponsorship | This work was supported by the Research Fund of the Sakarya University (Project No: 2019-5-19-174) and Sakarya University of Applied Sciences. | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Taylor & Francis Inc | en_US |
dc.relation.ispartof | Journal of Biomolecular Structure & Dynamics | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Phthalocyanine | en_US |
dc.subject | carbonic anhydrase | en_US |
dc.subject | cholinesterase | en_US |
dc.subject | enzyme inhibition | en_US |
dc.subject | molecular docking | en_US |
dc.subject | Silicon Iv Phthalocyanines | en_US |
dc.subject | Photodynamic Inactivation | en_US |
dc.subject | Metal-Complexes | en_US |
dc.subject | Zinc | en_US |
dc.subject | Electrochemistry | en_US |
dc.subject | Derivatives | en_US |
dc.subject | Inhibitors | en_US |
dc.subject | Acid | en_US |
dc.title | Phthalocyanine complexes with (4-isopropylbenzyl)oxy substituents: preparation and evaluation of anti-carbonic anhydrase, anticholinesterase enzymes and molecular docking studies | en_US |
dc.type | article | en_US |
dc.authorid | Guzel, Emre / 0000-0002-1142-3936 | |
dc.authorid | Gulcin, ilhami / 0000-0001-5993-1668 | |
dc.authorid | Taslimi, Parham / 0000-0002-3171-0633 | |
dc.department | Fakülteler, Teknoloji Fakültesi, Mühendislik Temel Bilimleri Bölümü | en_US |
dc.identifier.doi | 10.1080/07391102.2020.1818623 | |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.authorwosid | Guzel, Emre/H-2692-2018 | |
dc.authorwosid | Gulcin, ilhami/F-1428-2014 | |
dc.authorscopusid | 55579369300 | |
dc.authorscopusid | 57189006957 | |
dc.authorscopusid | 56658628800 | |
dc.authorscopusid | 35509141500 | |
dc.authorscopusid | 57205484281 | |
dc.authorscopusid | 8984510300 | |
dc.authorscopusid | 57203098758 | |
dc.identifier.wos | WOS:000571552700001 | en_US |
dc.identifier.scopus | 2-s2.0-85091308228 | en_US |
dc.identifier.pmid | 32954954 | en_US |