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Öğe Coumarin or benzoxazinone based novel carbonic anhydrase inhibitors synthesis molecular docking and anticonvulsant studies(Journal of Enzyme Inhibition and Medicinal Chemistry, 2016) Karataş, Mert Olgun; Uslu, Harun; Sarı, Suat; Alagöz, Mehmet Abdullah; Karakurt, Arzu; Alıcı, Bülent; Bilen, Çiğdem; Yavuz, Emre; Gençer, Nahit; Arslan, OktayAmong many others, coumarin derivatives are known to show human carbonic anhydrase (hCA) inhibitory activity. Since hCA inhibition is one of the underlying mechanisms that account for the activities of some antiepileptic drugs (AEDs), hCA inhibitors are expected to have antiseizure properties. There are also several studies reporting compounds with an imidazole and/or benzimidazole moiety which exert these pharmacological properties. In this study, we prepared fifteen novel coumarin-bearing imidazolium and benzimidazolium chloride, nine novel benzoxazinone-bearing imidazolium and benzimidazolium chloride derivatives and evaluated their hCA inhibitory activities and along with fourteen previously synthesized derivatives we scanned their anticonvulsant effects. As all compounds inhibited purified hCA isoforms I and II, some of them also proved protective against Maximal electroshock seizure (MES) and ScMet induced seizures in mice. Molecular docking studies with selected coumarin derivatives have revealed that these compounds bind to the active pocket of the enzyme in a similar fashion to that previously described for coumarin derivatives.Öğe Functionalized imidazolium and benzimidazolium salts as paraoxonase 1 inhibitors synthesis characterization and molecular docking studies(Bioorganic & Medicinal Chemistry, 2016) Karataş, Mert Olgun; Uslu, Harun; Alıcı, Bülent; Gökçe, Başak; Gençer, Nahit; Arslan, Oktay; Arslan, Nahide Burcu; Özdemir, NamıkParaoxonase (PON) is a key enzyme in metabolism of living organisms and decreased activity of PON1 was acknowledged as a risk for atherosclerosis and organophosphate toxicity. The present study describes the synthesis, characterization, PON1 inhibitory properties and molecular docking studies of functionalized imidazolium and benzimidazolium salts (1a–5g). The structures of all compounds were elucidated by IR, NMR, elemental analysis and structures of compounds 2b and 2c were characterized by single-crystal X-ray diffraction. Compound 1c, a coumarin substituted imidazolium salt showed the best inhibitory effect on the activity of PON1 with good IC50 value (6.37 lM). Kinetic investigation was evaluated for this compound and results showed that this compound is competitive inhibitor of PON1 with Ki value of 2.39 lM. Molecular docking studies were also performed for most active compound 1c and one of least active compound 2c in order to determine the probable binding model into active site of PON1 and validation of the experimental results.Öğe Functionalized imidazolium and benzimidazolium salts as paraoxonase 1 inhibitors: Synthesis, characterization and molecular docking studies(Pergamon-Elsevier Science Ltd, 2016) Karatas, Mert Olgun; Uslu, Harun; Alici, Bulent; Gokce, Basak; Gencer, Nahit; Arslan, Oktay; Arslan, N. BurcuParaoxonase (PON) is a key enzyme in metabolism of living organisms and decreased activity of PON1 was acknowledged as a risk for atherosclerosis and organophosphate toxicity. The present study describes the synthesis, characterization, PON1 inhibitory properties and molecular docking studies of functionalized imidazolium and benzimidazolium salts (1a-5g). The structures of all compounds were elucidated by IR, NMR, elemental analysis and structures of compounds 2b and 2c were characterized by single-crystal X-ray diffraction. Compound 1c, a coumarin substituted imidazolium salt showed the best inhibitory effect on the activity of PON1 with good IC50 value (6.37 mu M). Kinetic investigation was evaluated for this compound and results showed that this compound is competitive inhibitor of PON1 with K-1, value of 2.39 mu M. Molecular docking studies were also performed for most active compound 1c and one of least active compound 2c in order to determine the probable binding model into active site of PON1 and validation of the experimental results. (C) 2016 Elsevier Ltd. All rights reserved.Öğe In vitro inhibition effect of some coumarin compounds on purified human serum paraoxonase 1 (PON1)(Taylor & Francis Ltd, 2016) Gokce, Basak; Gencer, Nahit; Arslan, Oktay; Karatas, Mert Olgun; Alici, BulentHuman serum paraoxonase 1 (PON1; EC 3.1.8.1) is a high-density lipoprotein associated, calcium-dependent enzyme that hydrolyses aromatic esters, organophosphates and lactones and can protect the low-density lipoprotein against oxidation. In this study, in vitro effect of some hydroxy and dihydroxy ionic coumarin derivatives (1-20) on purified PON1 activity was investigated. Among these compounds, derivatives 11-20 are water soluble. In investigated compounds, compounds 6 and 13 were found the most active (IC50 = 35 and 34 mu M) for PON1, respectively. The present study has demonstrated that PON1 activity is very highly sensitive to studied coumarin derivatives.Öğe Inhibition of paraoxonase 1 by coumarin-substituted N-heterocyclic carbene silver(I), ruthenium(II) and palladium(II) complexes(Wiley, 2019) Karatas, Mert Olgun; Calgin, Gamze; Alici, Bulent; Gokce, Basak; Gencer, Nahit; Tok, Tugba Taskin; Arslan, OktayWe synthesized three coumarin-substituted benzimidazolium chlorides and their silver(I), ruthenium(II) and palladium(II) N-heterocyclic carbene (NHC) complexes. All compounds were characterized using appropriate spectroscopic techniques and elemental analyses. Single-crystal X-ray structure of a Pd(II)-NHC complex (6b) was also determined. The inhibitory properties of all compounds were tested on the activity of human paraoxonase 1 (PON1). All complexes exhibited weaker inhibitory properties than their corresponding benzimidazolium salts except for complex 6b which is the most active inhibitor with an IC50 value of 3.01 mu M among the compounds reported in this study. A kinetic evaluation showed that this complex inhibits PON1 activity in a non-competitive manner. Molecular docking studies were also performed for 6b in order to obtain more insight into the binding mode.Öğe Microwave-assisted synthesis of 1-substituted-1H-benzimidazolium salts: Non-competitive inhibition of human carbonic anhydrase I and II(Wiley-V C H Verlag Gmbh, 2019) Karlik, Ozgul; Gencer, Nahit; Karatas, Mert O.; Ergun, Adem; Cikrikci, Kubra; Arslan, Oktay; Alici, BulentA series of 1-substituted-1H-benzimidazolium p-toluenesulfonate salts were synthesized in good yields by the reaction of 1-substituted benzimidazole derivatives and p-toluenesulfonic acid under microwave irradiation. Two iodide salts were synthesized by the anion exchange reaction of the corresponding p-toluenesulfonate salt and NaI. All compounds were characterized by H-1 NMR, C-13 NMR, IR, LC-MS spectroscopic methods, and elemental analyses. The crystal structure of 1-methoxyethyl-1H-benzimidazolium p-toluenesulfonate 2d showed that cation and anion are interconnected by N-H center dot center dot center dot O and C-H center dot center dot center dot O hydrogen bonds. All compounds were examined as inhibitor of human carbonic anhydrase (hCA) I and II, and all of them inhibited hCA I and hCA II. Kinetic investigation results revealed that these compounds inhibit hCA I and hCA II in a non-competitive manner. The iodide salts had higher inhibitory activity than their corresponding p-toluenesulfonate salts.Öğe Some coumarins and benzoxazinones as potent paraoxonase 1 inhibitors(Taylor & Francis Ltd, 2016) Karatas, Mert Olgun; Uslu, Harun; Alici, Bulent; Gokce, Basak; Gencer, Nahit; Arslan, OktayIn this study, we aimed to investigate the effect of some coumarin and benzoxazinone derivatives on the activity of human PON1. Human serum paraoxonase 1 was purified from fresh human serum blood by two-step procedures that are ammonium sulfate precipitation (60-80%) and then hydrophobic interaction chromatography (Sepharose 4B, L-tyrosine and 1-napthylamine). The enzyme was purified 232-fold with a final specific activity of 27.1 U/mg. In vitro effects of some previously synthesized ionic coumarin or benzoxazinone derivatives (1-21) on purified PON1 activity were investigated. Compound 14 (1-(2,3,4,5,6)-pentamethyl-benzyl-3-(6,8-dimethyl-2H-chromen-2-one-4-yl)) benzimidazolium chloride was found out as the strongest inhibitor (IC50 = 7.84 mu M) for PON1 among the compounds. Kinetic investigation and molecular docking study were evaluated for one of the most active compounds (compound 12) and obtained data showed that this compound is competitive inhibitor of PON1 and interact with Leu262 and Ser263 in the active site of PON1. Moreover, coumarin derivatives were found out as the more potent inhibitors for PON1 than benzoxazinone derivatives.Öğe Some coumarins and benzoxazinones as potent paraoxonase 1 inhibitors(Journal of Enzyme Inhibition and Medicinal Chemistry, 2016) Karataş, Mert Olgun; Alıcı, Bülent; Gökçe, Başak; Gencer, Nahit; Arslan, Oktay; Uslu, HarunIn this study, we aimed to investigate the effect of some coumarin and benzoxazinone derivatives on the activity of human PON1. Human serum paraoxonase 1 was purified from fresh human serum blood by two-step procedures that are ammonium sulfate precipitation (60–80%) and then hydrophobic interaction chromatography (Sepharose 4B, L-tyrosine and 1-napthylamine). The enzyme was purified 232-fold with a final specific activity of 27.1 U/mg. In vitro effects of some previously synthesized ionic coumarin or benzoxazinone derivatives (1–21) on purified PON1 activity were investigated. Compound 14 (1-(2,3,4,5,6)-pentamethylbenzyl-3-(6,8-dimethyl-2H-chromen-2-one-4-yl))benzimidazolium chloride was found out as the strongest inhibitor (IC50 ¼ 7.84 mM) for PON1 among the compounds. Kinetic investigation and molecular docking study were evaluated for one of the most active compounds (compound 12) and obtained data showed that this compound is competitive inhibitor of PON1 and interact with Leu262 and Ser263 in the active site of PON1. Moreover, coumarin derivatives were found out as the more potent inhibitors for PON1 than benzoxazinone derivativesÖğe Synthesis, characterization and tyrosinase inhibitory properties of benzimidazole derivatives(Maik Nauka/Interperiodica/Springer, 2014) Karatas, Mert Olgun; Alici, Bulent; Cetinkaya, Engin; Bilen, Cigdem; Gencer, Nahit; Arslan, Oktay1-Alkylbenzimidazole and 1,3-dialkyl benzimidazolium salts were synthesized and characterized by the data of IR, H-1 NMR, C-13 NMR spectra and elemental analyses. These compounds were investigated as tyrosinase inhibitors. Tyrosinase has been purified from banana by affinity chromatography on a Sepharose 4B gel conjugated with L-tyrosine-p-aminobenzoic acid. All the synthesized compounds inhibited the tyrosinase activity. Among the compounds studied, 1,4-di(1H-benzo[d]imidazol-1-yl)butane was found to be the most active tyrosinase inhibitor (IC50 0.31 mM).
