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  • Küçük Resim
    Öğe
    In vitro inhibition effect of some chalcones on erythrocyte carbonic anhydrase I and II
    (Taylor & Francis Ltd, 2013) Gençer, Nahit; Bilen, Çiğdem; Demir, Dudu; Atahan, Alparslan; Ceylan, Mustafa; Küçükislamoğlu, Mustafa
    In this study, 4'-(phenylurenyl/thiourenyl) chalcones (14-25) were prepared from 4'-(phenylurenyl/thiourenyl)acetophenones and benzaldehyde derivatives by Claisen-Schmidt condensation. In vitro inhibition effects of chalcone derivatives on purified carbonic anhydrase I and carbonic anhydrase II were investigated by using the CO2 hydration method of Maren. The result showed that all the synthesized compounds inhibited the CA isoenzymes activity. 18 and 19 were found to be most active (IC50 = 25.41 m M and 23.06 mu M) for hCA I, respectively. For hCA II, 24 is the most active compound (IC50 = 14.40 mu M).
  • Küçük Resim
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    Synthesis, Biological Activity and Structure-Activity Relationship of Novel Diphenylurea Derivatives Containing Tetrahydroquinoline as Carbonic Anhydrase I and II Inhibitors
    (Wiley-V C H Verlag Gmbh, 2018) Atahan, Alparslan; Gençer, Nahit; Bilen, Çiğdem; Yavuz, Emre; Genç, Hayriye; Sönmez, Fatih; Küçükislamoğlu, Mustafa
    A series of novel tetrahydroquinoline derivatives containing urea moiety was synthesized and their invitro inhibitory effects on the human carbonic anhydrase isoenzymes (hCA-I and hCA-II) were evaluated by using the CO2 hydration method. All the synthesized compounds exhibited inhibitory activity against both hCA I and hCA II with 1-(4-fluorophenyl)-3-(4-(4-p-tolyl-5,6,7,8-tetrahydroquinolin-2-yl)phenyl)urea (7k, IC50 value of 5.28M and 5.51M, against hCA I and hCA II, respectively) as the strongest inhibitor in this study. Structure-activity relationships were also investigated. The results showed that most of synthesized compounds have a higher inhibitory activity against hCA I than hCA II. Also the substituents, containing two or more pairs of non-bonding electrons, generally increased the hCA I and II inhibitory activity. Furthermore, some electronic parameters such as the highest occupied molecular orbital and the lowest unoccupied molecular orbital (HOMO-LUMO) energy levels, electron affinity, total energy and dipole moments of the best inhibitors (7b, 7h and 7k) in this study were also calculated by using Gaussian software. The results revealed that HOMO-LUMO energy differences, total energy, chemical hardness and dipole moment of 7b, 7h and 7k showed a linear relationship with increasing inhibitory activity.
  • Küçük Resim
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    Synthesis, enzyme inhibition, and molecular docking studies of a novel chalcone series bearing benzothiazole scaffold
    (Wiley, 2023) Musatat, Ahmad Badreddin; Atahan, Alparslan; Ergün, Adem; Çıkrıkçı, Kübra; Gençer, Nahit; Arslan, Oktay; Zengin, Mustafa
    This study reports the facile synthesis of a novel series of benzothiazole-chalcones, in addition to their inhibitory profile on important metabolic enzymes including human carbonic anhydrases (hCA-I, hCA-II) and paraoxonase (PON-1). The inhibition parameters, IC50 (concentration for 50% inhibition) and Ki (dissociation constant) values, toward the title enzymes were determined for the studied compounds. As a result, IC50 values of hydratase activity were in the range 4.15-5.47 and 2.56-4.58 mu M for hCA-I and hCA-II, respectively. At the same time, IC50 values of esterase activity were in the range 24.91-104.00 and 35.25-97.00 mu M, while Ki values were in the range 14.43-59.66 and 26.65-73.34 mu M for hCA-I and hCA-II, respectively. In addition, PON-1 enzyme inhibition results showed interesting inhibitory effects, with IC50 values between 13.28 and 16.68 mu M. Finally, a comprehensive approach was established for the synthesized compounds based on theoretical calculations, which have been done using B3LYP, PBE0 theories and SVP, TVZP, TVZPP basis sets, followed by docking studies by which the outputs proved the harmonically flows with the experimental results.