Evaluation of carbonic anhydrase and paraoxonase inhibition activities and molecular docking studies of highly water-soluble sulfonated phthalocyanines

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dc.authoridGencer, Nahit/0000-0001-7092-8857
dc.authoridGuzel, Emre/0000-0002-1142-3936
dc.authoridCikrikci, Kubra/0000-0003-2276-1516
dc.authoridSonmez, Fatih/0000-0001-7486-6374
dc.authoridErgun, Adem/0000-0003-4647-6058
dc.contributor.authorGuzel, Emre
dc.contributor.authorSonmez, Fatih
dc.contributor.authorErkan, Sultan
dc.contributor.authorCikrikci, Kubra
dc.contributor.authorErgun, Adem
dc.contributor.authorGencer, Nahit
dc.contributor.authorArslan, Oktay
dc.date.accessioned2024-10-26T18:00:30Z
dc.date.available2024-10-26T18:00:30Z
dc.date.issued2020
dc.departmentSivas Cumhuriyet Üniversitesi
dc.description.abstractThe investigation of carbonic anhydrase and paraoxonase enzyme inhibition properties of water-soluble zinc and gallium phthalocyanine complexes (1 and 2) are reported for the first time. The binding of p-sulfonylphenoxy moieties to the phthalocyanine structure favors excellent solubilities in water, as well as providing an inhibition effect on carbonic anhydrase (CA) I and II isoenzymes and paraoxonase (PON I) enzyme. According to biological activity results, both complexes inhibited hCA I, hCA II, and PON1. Whereas 1 and 2 showed moderate hCA I and hCA II (off-target cytosolic isoforms) inhibitory activity (K-i values of 26.09 mu M and 43.11 mu M for hCA I and 30.95 mu M and 33.19 mu M for hCA II, respectively), they exhibited strong PON1 (associated with high-density lipoprotein [HDL]) inhibitory activity (K-i values of 0.37 mu M and 0.27 mu M, respectively). The inhibition kinetics were analyzed by Lineweaver-Burk double reciprocal plots. It revealed that 1 and 2 were noncompetitive inhibitors against PON1, hCA I, and hCA II. These complexes can be snore advantageous than other synthetic CA and PON inhibitors due to their water solubility. Docking studies were carried out to examine the interactions between hCA I, hCA II, and PON1 inhibitors and metal complexes at a molecular level and to predict binding energies.
dc.description.sponsorshipResearch Fund of Balikesir University [2020/080]; Sakarya University of Applied Sciences
dc.description.sponsorshipThis work was supported by the Research Fund of Balikesir University (Research Project no: 2020/080) and Sakarya University of Applied Sciences.
dc.identifier.doi10.3906/kim-2007-21
dc.identifier.endpage+
dc.identifier.issn1300-0527
dc.identifier.issue6
dc.identifier.pmid33488253
dc.identifier.scopus2-s2.0-85098600249
dc.identifier.scopusqualityQ3
dc.identifier.startpage1565
dc.identifier.trdizinid524243
dc.identifier.urihttps://doi.org/10.3906/kim-2007-21
dc.identifier.urihttps://search.trdizin.gov.tr/tr/yayin/detay/524243
dc.identifier.urihttps://hdl.handle.net/20.500.12418/27718
dc.identifier.volume44
dc.identifier.wosWOS:000599807000011
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakTR-Dizin
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTubitak Scientific & Technological Research Council Turkey
dc.relation.ispartofTurkish Journal of Chemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectPhthalocyanine
dc.subjectsulfonated
dc.subjectwater-soluble
dc.subjectparaoxonase
dc.subjectcarbonic anhydrase
dc.subjectenzyme inhibition
dc.subjectmolecular docking
dc.titleEvaluation of carbonic anhydrase and paraoxonase inhibition activities and molecular docking studies of highly water-soluble sulfonated phthalocyanines
dc.typeArticle

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