Novel eugenol derivatives: Potent acetylcholinesterase and carbonic anhydrase inhibitors

Topal, Fevzi; Gülçın, İlhami; Daştan, Arif; Güney, Murat

doi:10.1016/j.ijbiomac.2016.10.096

Cited by 111 publications

(76 citation statements)

References 74 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Carbonic anhydrase isoenzymes play a key role in many pathophysiological events including CO 2 /HCO 3 − transport and balance, biosynthesis reactions involving gluconeogenesis, urea synthesis, lipogenesis, respiration, calcification, tumorigenicity, electrolyte release in different tissues and organs, and bone resorption . CAs can be inhibited in the range of micromolar to nanomolar by sulfonamide and its derivatives .…”

Section: Discussionmentioning

confidence: 99%

“…However, some patients may be hypersensitive to sulfonamide and its derivatives. Recently, inhibition mechanism of several phenolic acids, phenols, or phenolic derivatives is detailed by our group on the CA isoenzymes . It has been reported that phenols bind to the CA isoenzymes in a different way from the inhibition mechanism of classical sulfonamides.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Inhibition properties of some flavonoids on carbonic anhydrase I and II isoenzymes purified from human erythrocytes

Huyut

Beydemır

Gülçın

2017

J Biochem Mol Toxicol

View full text Add to dashboard Cite

Carbonic anhydrases (CAs, E.C.4.2.1.1) play a critical role in many important physiological events and treatment of some diseases. Flavonoids or phenolic compounds have been discovered as novel CAs inhibitors instead of the traditional sulfonamides, with different binding to CAs, pro-drug activities, and new inhibition mechanisms. Here, we investigated the inhibition effects of some flavonoids including malvin, callistephin, oenin, pelargonin, silychristin, and 1-(4-methoxyphenyl)-2-methyl-3-nitro-1-H-indol-6-ol (ID-8) against hCA I and II, which purified from human erythrocytes by affinity column chromatography. Both hCA isoenzymes were inhibited by flavonoids, with IC and K values in the range of 2.34 nM to 346.5 μM and 51.01-99.55 μM for hCA I and 86.60-750.00 μM for hCA II, respectively. These results showed that flavonoids especially malvin and oenin effectively inhibited hCA I and II isoenzymes. Hence, they may be used as an effective CA inhibitor in medical applications for treatment of certain diseases such as glaucoma, in the future.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Inhibition properties of some flavonoids on carbonic anhydrase I and II isoenzymes purified from human erythrocytes

Huyut

Beydemır

Gülçın

2017

J Biochem Mol Toxicol

View full text Add to dashboard Cite

show abstract

“…Recently, the interactions of AChE and BChE with cyclic thioureas, hetaryl sulfonamides, Mannich bases, ureas derived from phenethylamines, tetrahydropyrimidines, diaryl ethers, β‐lactams, benzenesulfonamides, and tetrahydropyrimidine‐5‐carboxylates as well as the interactions for both CA isoenzymes with caffeic acid phenethyl ester, polyphenols and phenolic acids, benzotropones, bromophenols, dopaminergic compounds, sulfamides, sulfonamides, acylsulfonamides, benzenesulfonamides, 1,3,5‐trisubstituted‐pyrazolines,, tetralone‐based 1,4‐benzothiazepine derivatives, novel eugenol derivatives, some natural sulfonamide derivatives, and novel (3aR,4S,7R,7aS)‐2‐(4‐((E)‐3‐(3‐aryl)acryloyl) phenyl)‐3a,4,7,7a‐tetrahydro‐1H‐4,7‐methanoisoindole‐1,3(2H)‐dione derivatives benzylsulfamides have been studied.…”

Section: Discussionmentioning

confidence: 99%

Discovery of potent carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base

Taslimi

Osmanova

Gülçın

et al. 2017

J Biochem Mol Toxicol

View full text Add to dashboard Cite

Compounds containing nitrogen and sulfur atoms can be widely used in various fields, including industry, medicine, biotechnology, and chemical technology. Among them, amides of acids and heterocyclic compounds have an important place. These amides and thiazolidine-4-ones showed good inhibitory action against butyrylcholinesterase (BChE), acetylcholinesterase (AChE), and human carbonic anhydrase isoforms. AChE exists at high concentrations in the brain and red blood cells. BChE is an important enzyme that is plentiful in the liver, and it is released into the blood in a soluble form. They were demonstrated to have effective inhibition profiles with K values of 23.76-102.75 nM against hCA I, 58.92-136.64 nM against hCA II, 1.40-12.86 nM against AChE, and 9.82-52.77 nM against BChE. On the other hand, acetazolamide showed K value of 482.63 ± 56.20 nM against hCA I, and 1019.60 ± 163.70 nM against hCA II. Additionally, Tacrine inhibited AChE and BChE, showing K values of 397.03 ± 31.66 and 210.21 ± 15.98 nM, respectively.

show abstract

“…CA first purified from bovine erythrocytes [6,7], are found in tissues such as brain, lung, stomach, pancreas, liver, kidney, muscle tissue, and especially red blood cells [8,9]. It is one of the most important buffer systems in human body.…”

Section: Previous Studiesmentioning

confidence: 99%

“…Additionally, CA enzymes take part in vital functions such as diversity and workability [7][8][9][10] (Table 1), remarkable activities against CA I, and CA II in the ranges of 1.27-3.30 nM and 1.1-2.68 nM, respectively, were obtained.…”

Section: Cholinergic Enzymes Assaymentioning

confidence: 99%

Inhibition Effects of Some Lignans on Carbonic Anhydrase, Acetylcholinesterase and Butyrylcholinesterase Enzymes Leyla Polat Köse and İlhami Gülçin

Köse¹,

Gülçın²

2017

Rec.Nat.Prod.

Self Cite

View full text Add to dashboard Cite

Lignans are a large group of chemical compounds found in plants. They have effects on enzymes, protein synthesis, cell proliferation, angiogenesis, growth factor and cell differentiation. In this study, inhibition effects of α-(-)-conidendrin, enterodiole, enterolactone, nordihydroguaiaretic acid, secoisolariciresinol and secoisolariciresinol diglucoside against carbonic anhydrase I and II isoenzymes (CA I, and II) and acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes were investigated. The Ki values of the lignans were found to be in the ranges of 1.27-3.30 nM for CA I, 1.11-2.68 nM for CA II, 0.72-1.62 nM for AChE, and 0.08-0.20 nM for AChE.

show abstract

Novel eugenol derivatives: Potent acetylcholinesterase and carbonic anhydrase inhibitors

Cited by 111 publications

References 74 publications

Inhibition properties of some flavonoids on carbonic anhydrase I and II isoenzymes purified from human erythrocytes

Inhibition properties of some flavonoids on carbonic anhydrase I and II isoenzymes purified from human erythrocytes

Discovery of potent carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base

Inhibition Effects of Some Lignans on Carbonic Anhydrase, Acetylcholinesterase and Butyrylcholinesterase Enzymes Leyla Polat Köse and İlhami Gülçin

Contact Info

Product

Resources

About