The impact of some natural phenolic compounds on carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α‐glycosidase enzymes: An antidiabetic, anticholinergic, and antiepileptic study

Osmanova

Çağlayan

et al. 2018

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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.

Section: Discussionmentioning

confidence: 98%

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

Osmanova

Çağlayan

et al. 2018

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“…It has been reported that activating the cholinergic function by inhibiting AChE can be a clinically effective method for treatment of AD. AChE is the key enzymes that play important roles in cholinergic transmission by hydrolyzing the neurotransmitter ACh …”

Section: Resultsmentioning

confidence: 99%

Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes

Atmaca

Yıldırım

et al. 2018

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In this study, we aimed to determine the inhibition effects of novel synthesized sulfamates (2a-g), sulfonamides (3b-f), carbonyl sulfonamides (3h and i), and carbonyl sulfamates (4h and 4i), which were tested against two human cytosolic carbonic anhydrase I and II isozymes (hCA I and II) and acetylcholinesterase (AChE) enzyme. For inhibition properties of allylic sulfamates, the half maximal inhibitory concentration (IC ) and inhibition constant (K ) were calculated for each novel compounds. The allylic sulfamates showed that K values are in the range of 187.33-510.31 pM for hCA I, 104.22-290.09 pM against hCA II, and 12.73-103.63 pM against AChE. The results demonstrated that all newly synthesized compounds had shown effective inhibition against hCA I and II isoenzymes and AChE enzyme.

“…α‐Glycosidase inhibitory efficacy of novel N‐substituted tetrahydropyrimidines based on phenylthiourea ( 1a‐d ) was performed using p ‐nitrophenyl‐ d ‐glycopyranoside ( p ‐NPG) as the substrate, conforming to the method of Tao et al Samples were prepared by dissolving 20 mg in 20 mL (EtOH:H 2 O). First, 200 µL of phosphate buffer (PB) was mixed with 40 µL of the enzyme solution in PB (0.15 U/mL, pH 7.4) and 50 to 300 µL of the sample . Multiple solutions in PB were prepared in case of getting full enzyme inhibition.…”

Section: Experimental and Methodsmentioning

confidence: 99%

Synthesis, characterization, antioxidant, antidiabetic, anticholinergic, and antiepileptic properties of novel N‐substituted tetrahydropyrimidines based on phenylthiourea

Maharramova

Sujayev

et al. 2018

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In the presence of trifluoroacetic acid, on the basis of three‐component condensation of phenylthiourea with its salicylaldehyde and methyl‐3‐oxobutanoate, an efficient method for the synthesis of 1‐(4‐(2‐hydroxyphenyl)‐6‐methyl‐1‐phenyl‐2‐thioxo‐1,2,3,4‐tetrahydropyrimidin‐5‐yl)ethanone (I) has been worked out. These novel N‐substituted tetrahydropyrimidines based on phenylthiourea showed good inhibitory action against acetylcholinesterase (AChE), α‐glycosidase, and human carbonic anhydrase (hCA) isoforms I and II. K i values of AChE enzyme were in the range of 0.48 to 7.46 nM. The hCA I and II were effectively inhibited by the compounds, with K i values in the range of 502.44 to 923.11 nM for hCA I and 400.32 to 801.57 nM for hCA II, respectively. The antioxidant activity of the novel N‐substituted tetrahydropyrimidines based on phenylthiourea was investigated by using different in vitro antioxidant assays; including 1,1‐diphenyl‐2‐picrylhydrazyl (DPPH·) radical scavenging, Cu 2+ and Fe 3+ reducing activities.