Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan &amp;beta;-Lactam Derivatives

Genc, Hayriye; Kalın, Ramazan; Köksal, Zeynep; Sadeghian, Nastaran; Koçyiğit, Ümit M.; Zengin, Mustafa; Gülçın, İlhami; Özdemir, Haşan

doi:10.20944/preprints201609.0123.v1

Cited by 21 publications

(19 citation statements)

References 70 publications

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“…To determine K m and V max values for LPO, activity was measured at 412 nm (20°C and pH 6.0) for five different substrates concentrations . For this purpose, generally 0.2–1.5 mL volumes from stock solution of the substrates were used.…”

Section: Methodsmentioning

confidence: 99%

The inhibition effects of some natural products on lactoperoxidase purified from bovine milk

Köksal

Kalın

Gerni

et al. 2017

J Biochem Mol Toxicol

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In this study, inhibition profiles of some natural products, which are digoxin, L-Dopa, dopamine, isoliquiritigenin, and 1,1,2,2-tetrakis(p-hydroxyphenyl)ethane (Tetrakis), were investigated against bovine lactoperoxidase (LPO) enzyme. Digoxin, L-Dopa, and dopamine are active ingredients of some drugs, which have important functions in our body, especially in cases of heart failure. Isoliquiritigenin and tetrakis are types of natural phenolic compounds, which play an important role in cancer prevention and treatment. LPO enzyme was purified from bovine milk using sepharose-4B-l-tyrosine sulfonamide affinity column chromatography. LPO is responsible for the nonimmune biological defense system and has antibacterial activity so selection of these active substances is important. The inhibition studies are performed with the ABTS substrate. Bovine LPO enzyme was effectively inhibited by phenolic molecules. K values of these natural products were found as 0.20 ± 0.09, 0.22 ± 0.17, 0.49 ± 0.11, 0.49 ± 0.27, and 1.20 ± 0.25 μM, respectively. Tetrakis and digoxin exhibited noncompetitive inhibition, and other molecules showed competitive inhibition.

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Section: Methodsmentioning

confidence: 99%

The inhibition effects of some natural products on lactoperoxidase purified from bovine milk

Köksal

Kalın

Gerni

et al. 2017

J Biochem Mol Toxicol

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“…BChE and AChE activities were measured according to Ellmanʼs procedure [36] as described previously [37][38][39] . AChE (C2888-500UN;…”

Section: Ache and Bche Activitiesmentioning

confidence: 99%

Novel amides of 1,1‐bis‐(carboxymethylthio)‐1‐arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties

Taslimi

Osmanova

Çağlayan

et al. 2018

J Biochem & Molecular Tox

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The thiolation reaction was carried out in a benzene solution at 80°C and p-substituted ketones and mercaptoacetic acid in a molar ratio (1:4) of in the presence of a catalytic amount of toluene sulfonic acids. The enzyme inhibition activities of the novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes derivatives were investigated. These novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes derivatives showed good inhibitory action against acetylcholinesterase (AChE) butyrylcholinesterase (BChE), and human carbonic anhydrase I and II isoforms (hCA I and II). AChE inhibitors, interacting with the enzyme as their primary target, are applied as relevant drugs and toxins. Many clinically established drugs are carbonic anhydrase inhibitors, and it is highly anticipated that many more will eventually find their way into the market. The novel synthesized compounds inhibited AChE and BChE with K values in the range of 0.64-1.47 nM and 9.11-48.12 nM, respectively. On the other hand, hCA I and II were effectively inhibited by these compounds, with K values between 63.27-132.34 and of 29.63-127.31 nM, respectively.

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“…Protein values were assessed by measuring 280 nm absorbance fractions. Also, all elutes were measured for CO 2 ‐hydratase activity …”

Section: Methodsmentioning

confidence: 99%

Inhibitory effects of some drugs on carbonic anhydrase enzyme purified from Kangal Akkaraman sheep in Sivas, Turkey

Koçyiğit

Daştan

Taslimi

et al. 2017

J Biochem & Molecular Tox

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In this study, carbonic anhydrase (CA) enzyme was purified and characterized from blood samples of Kangal Akkaraman sheep and inhibitory properties on certain antibiotics were examined. CA purification was composed of preparation of the hemolysate and conducting the Sepharose-4B-tyrosine-sulfanilamide affinity gel chromatography in having specific activity of 11626 EU mg −1 , yield of 14.40%, and 242.76-fold purification. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was performed to assess the enzyme purity and a single band was observed. Some antibiotics were exhibited in vitro inhibition on the CA activity. IC 50 values of these inhibitors were calculated by plotting activity percentage. IC 50 values of certain drugs (dexamethasone; caffeine; metamizole sodium; tetramisol; ceftiofur HCl; ivermectin; tavilin 50; penokain G; neosym; and sulfamezathine) were found as 0. 38, 8.24, 285.53, 114.77, 5.33, 2.76, 27.58, 213.50, 208.28, and 36.60 M, respectively. K i values of different drugs on Kangal Akkaraman sheep blood CA activity were found in the range of 0.21 ± 0.038-266.64 ± 37.11 M.

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Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives

Cited by 21 publications

References 70 publications

The inhibition effects of some natural products on lactoperoxidase purified from bovine milk

The inhibition effects of some natural products on lactoperoxidase purified from bovine milk

Novel amides of 1,1‐bis‐(carboxymethylthio)‐1‐arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties

Inhibitory effects of some drugs on carbonic anhydrase enzyme purified from Kangal Akkaraman sheep in Sivas, Turkey

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