The 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 (PON1) 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 (Ki values of µM and µM for hCA I and µM and µM for hCA II, respectively), they exhibited strong PON1 (associated with high-density lipoprotein [HDL]) inhibitory activity (Ki values of µM and µM, respectively). | Turkish Journal of Chemistry Turk J Chem 2020 44 1565-1573 http chem TÜBİTAK Research Article doi kim-2007-21 Evaluation of carbonic anhydrase and paraoxonase inhibition activities and molecular docking studies of highly water-soluble sulfonated phthalocyanines 1 2 3 4 Emre GÜZEL Fatih SÖNMEZ Sultan ERKAN Kübra ÇIKRIKÇI 4 4 4 5 Adem ERGÜN Nahit GENÇER Oktay ARSLAN Makbule B. KOÇAK 1 Department of Fundamental Sciences Faculty of Technology Sakarya University of Applied Sciences Sakarya Turkey 2 Pamukova Vocational School Sakarya University of Applied Sciences Sakarya Turkey 3 Chemistry and Chemical Processing Technologies Yıldızeli Vocational School Sivas Cumhuriyet University Sivas Turkey 4 Department of Chemistry Faculty of Arts and Science Balıkesir University Balıkesir Turkey 5 Department of Chemistry Faculty of Arts and Science İstanbul Technical University İstanbul Turkey Received Accepted Published Online Final Version Abstract The 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 PON1 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 Ki values of µM and µM for hCA I and µM and µM for hCA II respectively they exhibited strong PON1 associated with high-density lipoprotein HDL inhibitory activity Ki values of µM and µM respectively . The inhibition kinetics were analyzed by Lineweaver Burk double reciprocal plots. It revealed that 1 and 2 were noncompetitive inhibitors against .
