Synthesis and paroxonase activities of novel bromophenols

Akbaba, Yusuf; Türkeş, Cüneyt; Polat, Leyla Özgür; Söyüt, Hakan; Şahin, Ertan; Menzek, Abdullah; Göksu, Süleyman; Beydemır, Şükrü

doi:10.3109/14756366.2012.715287

Cited by 52 publications

(35 citation statements)

References 25 publications

(34 reference statements)

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“…K i values were calculated from Lineweaver-Burk graphs (Figures 1, 2 and 3), and both the K i and IC 50 parameters of the taxifolin were determined in this study. The Lineweaver-Burk plot is a graphical representation of the Lineweaver-Burk equation of enzyme kinetics 104 . The plot provides a useful graphical method for analysis of the Michaelis-Menten equation:…”

Section: Resultsmentioning

confidence: 99%

Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin

Göçer

Topal

et al. 2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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Taxifolin, also known as dihydroquercetin, is a flavonoid commonly found in plants. Carbonic anhydrase (CA, EC 4.2.1.1) plays an important role in many critical physiological events including carbon dioxide (CO 2 )/bicarbonate (HCO À 3 ) respiration and pH regulation. There are 16 known CA isoforms in humans, of which human hCA isoenzymes I and II (hCA I and II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of taxifolin against the slow cytosolic isoenzyme hCA I, and the ubiquitous and dominant rapid cytosolic isoenzyme hCA II were studied. Taxifolin, as a naturally bioactive flavonoid, has a K i of 29.2 nM against hCA I, and 24.2 nM against hCA II. For acetylcholinesterase enzyme (AChE) inhibition, K i parameter of taxifolin was determined to be 16.7 nM. These results clearly show that taxifolin inhibited both CA isoenzymes and AChE at the nM levels.

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Section: Resultsmentioning

confidence: 99%

Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin

Göçer

Topal

et al. 2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…For instance, we purified PON1 enzyme from human serum by using chromatographic methods. We obtained with a yield of 42.1%, specific activity of 3584 EU/mg proteins and approximately 229‐fold . Subsequently, we studied the effects of novel synthesized bromophenols on paraoxonase activity of human PON1.…”

Section: Discussionmentioning

confidence: 99%

A potential risk factor for paraoxonase 1: in silico and in-vitro analysis of the biological activity of proton-pump inhibitors†

Türkeş

2019

Journal of Pharmacy and Pharmacology

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Objectives Proton‐pump inhibitors (PPIs) are drugs commonly utilized by about 7% of adults in the world. Recent researches have shown that there are countless and severe side effects of these drugs. This situation has raised concern among clinicians and patients alike. The purpose of this study is to contribute the novel drug discovery and development technology and toxicology field by researching interactions of PPIs on paraoxonase 1. Methods In this study, the paraoxonase 1 enzyme was purified from human serum by using rapid and straightforward chromatographic techniques. Subsequently, the inhibition effects of pantoprazole, omeprazole, and esomeprazole, PPIs, were investigated on paraoxonase 1. Besides, molecular docking studies were performed to unravel the binding mechanism between the enzyme and drugs. Key findings All drugs showed potent inhibitory activities. IC50 of the drugs values were 54.780 ± 0.524, 86.470 ± 0.818 and 93.390 ± 0.885 mm and Ki constants were found as 39.895 ± 0.005 mm, 70.112 ± 0.010 mm and 78.868 ± 0.008 mm, respectively. The binding scores observed in silico studies were found to agree with the obtained from in‐vitro experimental results. Conclusions We observed that the drugs decreased PON1 activity at low concentrations. The results show that adjusting the dosages of these medications is a crucial case for each patient. The physicians should more carefully interpret whether there is an essential indication before prescribing PPIs and, if there is, to approve the proper dosing for the situation.

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“…The paraoxonase (PON) enzyme family consist of three members: PON1, PON2 and PON3 PON1 is the most studied enzyme of this family within mammalian enzymes. This enzyme is related to high‐density lipoprotein (HDL), which is calcium dependent and has a molecular weight of 43–45 kDa …”

Section: Introductionmentioning

confidence: 99%

The behaviour of some antihypertension drugs on human serum paraoxonase-1: an important protector enzyme against atherosclerosis

Demir

2019

Journal of Pharmacy and Pharmacology

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Objectives Paraoxonase‐1 (PON1) enzyme is related to high‐density lipoprotein (HDL), which is calcium dependent. It has essential roles such as protecting LDL against oxidation and detoxification of highly toxic substances. It is a significant risk to reduce the levels of this enzyme in patients with diabetes mellitus, cardiovascular diseases, hyperthyroidism and chronic renal failure. Methods Here, it was reported that the purification of human serum PON1 using straightforward methods and determination of the interactions between some antihypertension drugs and the enzyme. Key finding It was found that these drugs exhibit potential inhibitor properties for human serum PON1 with IC50 values in the range of 131.40–369.40 μm and Ki values in the range of 56.24 ± 6.75–286.74 ± 28.28 μm. These drugs showed different inhibition mechanisms. It was determined that midodrine and nadolol were exhibited competitive inhibition, but atenolol and pindolol were exhibited non‐competitive inhibition. Conclusion Usage of these drugs would be hazardous in some cases.

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Synthesis and paroxonase activities of novel bromophenols

Cited by 52 publications

References 25 publications

Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin

Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin

A potential risk factor for paraoxonase 1: in silico and in-vitro analysis of the biological activity of proton-pump inhibitors†

The behaviour of some antihypertension drugs on human serum paraoxonase-1: an important protector enzyme against atherosclerosis

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