Yazar "Supuran, Claudiu T." seçeneğine göre listele

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    Preparation, carbonic anhydrase enzyme inhibition and antioxidant activity of novel 7-amino-3,4-dihydroquinolin-2(1H)-one derivatives incorporating mono or dipeptide moiety
    (Taylor & Francis Ltd, 2020) Kucukbay, Hasan; Gonul, Zeynep; Kucukbay, F. Zehra; Angeli, Andrea; Bartolucci, Gianluca; Supuran, Claudiu T.
    New dipeptide-dihydroquinolinone derivatives were successfully synthesised by benzotriazole mediated nucleophilic acyl substitution reaction and their structures were elucidated by spectroscopic and analytic techniques. The carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activity of the new compounds was determined against four human (h) isoforms, hCA I, hCA II, hCA IX and hCA XII. While all compounds showed moderate to good in vitro CA inhibitory properties against hCA IX and hCA XII with inhibition constants in the micromolar level (37.7-86.8 and 2.0-8.6 mu M, respectively), they did not show inhibitory activity against hCA I and hCA II up to 100 mu M concentration. The antioxidant capacity of the peptide-dihydroquinolinone conjugates was determined using 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging method. Most of the synthesised compounds showed low antioxidant activities compared to the control antioxidant compounds BHA and alpha-tocopherol.
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    Synthesis and carbonic anhydrase I, II, IV and XII inhibitory properties of N-protected amino acid - sulfonamide conjugates
    (Taylor & Francis Ltd, 2016) Kucukbay, F. Zehra; Kucukbay, Hasan; Tanc, Muhammet; Supuran, Claudiu T.
    N-protected amino acids (Gly, Ala and Phe protected with Boc and Z groups) were reacted with sulfonamide derivatives, leading to the corresponding N-protected amino acid-sulfonamide conjugates. The carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activity of the new compounds was assessed against four human (h) isoforms, hCA I, hCA II, hCA IV and hCA XII. Among them, hCA II, IV and XII are antiglaucoma drug targets, being involved in aqueous humor secretion within the eye. Low nanomolar inhibition was measured against all four isoforms with the 20 reported sulfonamides, but no selective inhibitory profiles, except for some CA XII-selective derivatives, were observed. hCA I, II and XII were generally better inhibited by sulfonamides incorporating longer scaffolds and Gly/Ala, whereas the best hCA IV inhibitors were homosulfanilamide derivatives, incorporating Phe moieties. The amino acid-sulfonamide conjugates show good water solubility and effective hCA II, IV and XII inhibition, and may be considered as interesting candidates for antiglaucoma studies.
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    Synthesis and carbonic anhydrase inhibitory properties of amino acid - coumarin/quinolinone conjugates incorporating glycine, alanine and phenylalanine moieties
    (Taylor & Francis Ltd, 2016) Kucukbay, F. Zehra; Kucukbay, Hasan; Tanc, Muhammet; Supuran, Claudiu T.
    N-Protected amino acids (Gly, Ala and Phe) were reacted with amino substituted coumarin and quinolinone derivatives, leading to the corresponding N-protected amino acid-coumarin/quinolinone conjugates. The carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activity of the new compounds was assessed against various human (h) isoforms, such as hCA I, hCA II, hCA IV and hCA XII. The quinolinone conjugates were inactive as enzyme inhibitors, whereas the coumarins were ineffective hCA I/II inhibitors (K(I)s>50 mu M) but were submicromolar hCA IV and XII inhibitors, with inhibition constants ranging between 92 nM and 1.19 mu M for hCA IV, and between 0.11 and 0.79 mu M for hCA XII. These coumarin derivatives, as many others reported earlier, thus show an interesting selective inhibitory profile for the membrane-bound over the cytosolic CA isoforms.
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    Synthesis and human carbonic anhydrase I, II, VA, and XII inhibition with novel amino acid-sulphonamide conjugates
    (Taylor & Francis Ltd, 2020) Kucukbay, Hasan; Bugday, Nesrin; Kucukbay, F. Zehra; Ageli, Andrea; Bartolucci, Gianluca; Supuran, Claudiu T.
    A series of amino acid-sulphonamide conjugates was prepared through benzotriazole mediated coupling reactions and characterised by H-1-NMR, C-13-NMR, MS, and FTIR spectroscopic techniques as well as elemental analysis. The carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activity of the new compounds was determined against four human (h) isoforms, hCA I, hCA II, hCA VA, and hCA XII. Most of the synthesised compounds showed effective in vitro CA inhibitory properties. The new amino acid-sulphonamide conjugates showed potent inhibitory activity against hCA II, some of them at subnanomolar levels, exhibiting more effective inhibitory activity compared to the standard drug acetazolamide. Some of these sulphonamides were also found to be effective inhibitors of hCA I, hCA VA, and hCA XII, with activity from the low to high nanomolar range.
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    Synthesis carbonic anhydrase enzyme inhibition and antioxidant activity of novel benzothiazole derivatives incorporating glycine, methionine, alanine, and phenylalanine moieties
    (Taylor & Francis Ltd, 2019) Payaz, Deniz Uzeroglu; Kucukbay, F. Zehra; Kucukbay, Hasan; Angeli, Andrea; Supuran, Claudiu T.
    Thirteen novel benzothiazole derivatives incorporating glycine, methionine, alanine, and phenylalanine were synthesised by facile acylation reactions through benzotriazole or DCC mediated reactions and their structures were identified by H-1-NMR, 13C-NMR, and FT-IR spectroscopic techniques and elemental analysis. The carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activity of the new compounds was assessed against four human (h) isoforms, hCA I, hCA II, hCA V, and hCA XIII. Some of the synthesised compounds showed good in vitro carbonic anhydrase inhibitory properties, with inhibition constants in the micromolar level. The new amino acid benzothiazole conjugates found to be more effective against hCA V and hCA II inhibition. In vitro antioxidant activities of the novel compounds were determined by DPPH method. Most of the synthesised compounds showed moderate to low antioxidant activities compared to the control antioxidant compounds (BHA and alpha-tocopherol).
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    Synthesis of new 7-amino-3,4-dihydroquinolin-2(1H)-one-peptide derivatives and their carbonic anhydrase enzyme inhibition, antioxidant, and cytotoxic activities
    (Wiley-V C H Verlag Gmbh, 2021) Kucukbay, Hasan; Gonul, Zeynep; Kucukbay, Fatumetuzzehra Zehra; Tekin, Zehra; Angeli, Andrea; Bartolucci, Gianluca; Supuran, Claudiu T.
    Six new monopeptides, seven new dipeptides, and two deprotected monopeptide dihydroquinolinone conjugates were prepared by the benzothiazole-mediated method and their structures were confirmed by nuclear magnetic resonance, mass, infrared spectroscopy, and elemental analysis methods. The human carbonic anhydrase (hCA) I and hCA II enzyme inhibition activities of the compounds were determined using the stopped-flow instrument. The synthesized peptide-dihydroquinolinone conjugates 2, 3, 6, 10, 13, and 15 showed inhibition against the hCA II enzyme in the range of 15.7-65.7 mu M. However, none of the compounds showed inhibition of hCA I at a concentration of 100 mu M. The antioxidant activities of the compounds were also examined using the DPPH (2,2-diphenyl-1-picrylhydrazyl) radical scavenging method at concentrations of 12.5-125 mu g/ml, but when compared with the standard antioxidant compounds alpha-tocopherol and butylated hydroxyanisole (BHA), weak antioxidant activities were detected. The cytotoxic effects of four compounds against the A549 and BEAS-2B cell lines were also investigated. Among the compounds studied, compound 7 was found to be most effective, with the IC50 values on the A549 cells for 48 and 72 h being 26.87 and 9.979 mu g/ml, respectively, and the IC50 values on the BEAS-2B cells being >100 mu g/ml. None of the tested compounds showed antimicrobial activity in the concentration range (800-1.56 mu g/ml) studied.
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    Synthesis, antioxidant and carbonic anhydrase inhibitory properties of monopeptide-anthraquinone conjugates
    (Acg Publications, 2021) Kucukbay, Hasan; Parladi, F. Muzeyyen; Kucukbay, F. Zehra; Angeli, Andrea; Bartolucci, Gianluca; Supuran, Claudiu T.
    Novel monopeptide-anthraquinone conjugates (1-16) were synthesized by the reaction of appropriate N-protected amino acid with 2-hydroxymethylanthraquinone in good or high yields. The structural elucidation of the new compounds was accomplished by H-1 NMR, C-13 NMR, MS, FT-IR spectroscopy and elemental analysis techniques. The carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activity of the new compounds was determined against two human (h) isoforms, hCA I and hCA II. While three of the sixteen compounds showed moderate in vitro carbonic anhydrase inhibitory properties against hCA II with inhibition constants in the micromolar level (43.5, 67.4 and 78.1 mu M), they did not show inhibitory activity against hCA I up to 100 mu M concentration. The antioxidant abilities of the compounds were determined using the 1,1-diphenyl-2-picrylhydrazil (DPPH) radical scavenging method, ferric ion reducing assay and metal chelation methods. While a small amount of antioxidant activity was observed according to the DPPH and ferric ion reducing power assay methods, none of the compounds showed antioxidant properties according to the metal chelating activity method at the concentrations studied.
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    Synthesis, characterization and carbonic anhydrase inhibitory activity of novel benzothiazole derivatives
    (Taylor & Francis Ltd, 2016) Kucukbay, F. Zehra; Bugday, Nesrin; Kucukbay, Hasan; Tanc, Muhammet; Supuran, Claudiu T.
    N-protected amino acids were reacted with substituted benzothiazoles to give the corresponding N-protected amino acid-benzothiazole conjugates (60-89%). Their structures were confirmed by proton nuclear magnetic resonance (H-1 NMR), carbon-13 nuclear magnetic resonance (C-13 NMR), IR and elemental analysis. Their carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activities were determined against two cytosolic human isoforms (hCA I and hCA II), one membrane-associated (hCA IV) and one transmembrane (hCA XII) enzyme by a stopped-flow CO2 hydrase assay method. The new compounds showed rather weak, micromolar inhibitory activity against most of these enzymes.