Synthesis and carbonic anhydrase inhibitory properties of novel coumarin derivatives

Karataş, Mert Olgun; Alıcı, Bülent; Çakır, Ümit; Çetinkaya, Engin; Demir, Dudu; Ergün, Adem; Gençer, Nahit; Arslan, Oktay

doi:10.3109/14756366.2012.677838

Cited by 28 publications

(18 citation statements)

References 39 publications

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“…Therefore, it had been reported that some 6,7-dihydroxy-3-aryl coumarin derivatives inhibited PON 1 in another paper 18 . We had reported CA inhibitory properties of compounds 1-20 in our previous studies 19,20 and these compounds have good IC 50 values for CA which are in the micromolar range. In this article, compounds 1-20 are ionic compounds but they have apolar character and dissolve in water partly.…”

Section: Resultsmentioning

confidence: 99%

“…So lactam derivatives and a coumarin were not hydrolyzed by PON1. In our study, synthesized compounds are bearing both hydroxy and azolium substituent so according to the results of our and previous studies, compounds [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] are not suitable substrate for PON1 and they inhibited PON1 effectively.…”

Section: Resultsmentioning

confidence: 99%

“…According to these results, the addition of a benzene ring to structure increased lipophilicity of compounds and making them more active than other coumarin derivatives. For the comparison of benzimidazolium salts, we can classify them in two parts; (i) 7-hydroxy coumarin (3)(4)(5)(6)(7)(8) and (ii) 7,8-dihydroxy coumarin-bearing compounds (11)(12)(13)(14)(15)(16)(17)(18)(19)(20). Some compounds are bearing same groups in their structures apart from coumarin scaffold.…”

Section: Resultsmentioning

confidence: 99%

“…These compounds had been synthesized and CA inhibitory properties of these compound had been reported previously 19,20 . Compounds 1-10 are 7-hydroxy coumarin derivatives and compounds 11-20 are 7,8-dihydroxy coumarin derivatives.…”

Section: Resultsmentioning

confidence: 99%

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In vitro inhibition effect of some coumarin compounds on purified human serum paraoxonase 1 (PON1)

Gökçe

Gençer

Arslan

et al. 2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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Human 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 (IC 50 ¼ 35 and 34 mM) for PON1, respectively. The present study has demonstrated that PON1 activity is very highly sensitive to studied coumarin derivatives.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

In vitro inhibition effect of some coumarin compounds on purified human serum paraoxonase 1 (PON1)

Gökçe

Gençer

Arslan

et al. 2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…Enzyme inhibition is an important issue for drug design and biochemical applications [45][46][47] . In this study, we have showed that human PON1 was inhibited effectively by some coumarin or benzoxazinone derivatives.…”

Section: Resultsmentioning

confidence: 99%

Some coumarins and benzoxazinones as potent paraoxonase 1 inhibitors

Karataş

Uslu

Alıcı

et al. 2016

Journal of Enzyme Inhibition and Medicinal Chemistry

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In 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 (IC 50 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 derivatives.

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Microwave‐assisted synthesis of 1‐substituted‐1H‐benzimidazolium salts: Non‐competitive inhibition of human carbonic anhydrase I and II

Karlık

Gençer²,

Karataş

et al. 2019

Archiv der Pharmazie

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A 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 1 H NMR, 13 C NMR, IR, LC-MS spectroscopic methods, and elemental analyses. The crystal structure of 1-methoxyethyl-1Hbenzimidazolium p-toluenesulfonate 2d showed that cation and anion are interconnected by N−H···O and C−H···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.

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Synthesis and carbonic anhydrase inhibitory properties of novel coumarin derivatives

Cited by 28 publications

References 39 publications

In vitro inhibition effect of some coumarin compounds on purified human serum paraoxonase 1 (PON1)

In vitro inhibition effect of some coumarin compounds on purified human serum paraoxonase 1 (PON1)

Some coumarins and benzoxazinones as potent paraoxonase 1 inhibitors

Microwave‐assisted synthesis of 1‐substituted‐1H‐benzimidazolium salts: Non‐competitive inhibition of human carbonic anhydrase I and II

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