The first synthesis of 4-phenylbutenone derivative bromophenols including natural products and their inhibition profiles for carbonic anhydrase, acetylcholinesterase and butyrylcholinesterase enzymes

J Biochem & Molecular Tox

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: Introductionmentioning

confidence: 99%

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

J Biochem & Molecular Tox

Osmanova

Çağlayan

et al. 2018

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“…Recently, the cloning of genomes of multitude microorganisms, such as fungi, pathogenic bacteria, and protozoa, has advanced enormously . The feasibility to record intermittent pathways for inhibiting virulence agents or proteins necessary for the life cycle of such pathogens factors, among which the CAs, have received significant attention . All the synthesized compounds were tested for the investigation of their inhibitory activity toward the hCA I and II isoforms and AChE enzyme.…”

Section: Resultsmentioning

confidence: 99%

“…The hCA I is abundant in erythrocytes and is observed in many tissues, but its accurate physiological function is not known. CA I is dependent on retinal edema and cerebral edema, and the inhibition of CA I can be a noteworthy factor in confrontation to these positions The physiologically predominant cytosolic isoenzyme hCA II is associated with diverse diseases.…”

Section: Resultsmentioning

confidence: 99%

“…The entire range of the compounds showed highly impressive hCA II inhibitory activity compared to that of AZA molecule. As can be observed in CA II, the most inhibition effect of CA II was recorded by 1h rel ‐(1 R ,2 S ,3 R ,4 S ,6 S )‐2,4,6‐tris(4‐bromophenyl)‐4‐hydroxycyclohexane‐1,3‐diyl)bis((4‐bromophenyl)methanone) with the K i amount of 18.77 ± 5.10 nM (Figure ). AD includes neurodegeneration resulting in personality variations, memory impairment, and emotional perturbation . Thus, one significant purpose to retard the progress of signs of AD is the alteration of the cholinergic function.…”

Section: Resultsmentioning

confidence: 99%

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Evaluation of acetylcholinesterase and carbonic anhydrase inhibition profiles of 1,2,3,4,6-pentasubstituted-4-hydroxy-cyclohexanes

Koçyiğit

Gülçın

et al. 2017

J Biochem Mol Toxicol

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Carbonic anhydrase (CA; EC 4.2.1.1) is used for remedial purposes for several years, as there is significant focus on expanding more new activators (CAAs) and high affinity inhibitors. Alzheimer's disease and other similar ailments such as dementia and vascular dementia with Lewy bodies reduce cholinergic activity in the important areas involved in cognition and memory. Prevalent drugs for the symptomatic therapy of dementia are significant in increasing the associated cholinergic deficiency by inhibiting acetylcholinesterase (AChE). These six-membered carbocycles showed nice inhibitory action against AChE and human carbonic anhydrase (hCA) II and I isoforms. The hCA I, II, and AChE were efficiently inhibited by these molecules, with K values in the range of 6.70-35.85 nM for hCA I, 18.77-60.84 nM for hCA II, and 0.74-4.60 for AChE, respectively.

“…[33] CA isoenzymes' activity investigation was obtained using the spectrophotometric style of Verpoorte et al [34] as described before. One enzyme unit of esterase activity of CA is the amount of enzyme that cause the pH of a 20 mM Trizma buffer to drop from 8.3 to 6.3 per minute at 0 • C. [36] For estimation of protein quantity, the Bradford procedure [35] was used during the separation stages.…”

Section: Biochemistry Studies 251 Both Hca Isoenzymes Purification mentioning

confidence: 99%

Synthesis, crystal structure and biological evaluation of spectroscopic characterization of Ni(II) and Co(II) complexes with N‐salicyloil‐N′‐maleoil‐hydrazine as anticholinergic and antidiabetic agents

Gondolova

J Biochem & Molecular Tox

Medjidov

et al. 2018

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[Ni(C H N O ) (H O) ]•3(C H NO) (1) and [Co(C H N O ) (H O) ]•3(C H NO) (2) are synthesized and characterized by elemental analysis, FT-IR spectra, magnetic susceptibility, and thermal analysis. In addition, the crystal structure of Ni(II) complex is presented. Both complexes show distorted octahedral geometry. In 1 and 2, metal ions are coordinated by two oxygen atoms of salicylic residue and two nitrogen atoms of maleic amide residue from two ligands, and two oxygen atoms from two water molecules. In this paper, both compounds showed excellent inhibitory effects against human carbonic anhydrase (hCA) isoforms I, and II, α-glycosidase, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). Compounds 1 and 2 had Ki values of 18.36 ± 4.38 and 26.61 ± 7.54 nM against hCA I and 13.81 ± 3.02 and 29.56 ± 6.52 nM against hCA II, respectively. On the other hand, their Ki values were found to be 487.45 ± 54.18 and 453.81 ± 118.61 nM against AChE and 199.21 ± 50.35 and 409.41 ± 6.86 nM against BChE, respectively.