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

The thiolation reaction was carried out in a benzene solution at 80 degrees 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-i 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-i values between 63.27-132.34 and of 29.63-127.31 nM, respectively

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

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-i values of 23.76-102.75nM against hCA I, 58.92-136.64nM against hCA II, 1.40-12.86nM against AChE, and 9.82-52.77nM against BChE. On the other hand, acetazolamide showed K-i value of 482.63 +/- 56.20nM against hCA I, and 1019.60 +/- 163.70nM against hCA II. Additionally, Tacrine inhibited AChE and BChE, showing K-i values of 397.03 +/- 31.66 and 210.21 +/- 15.98nM, respectively

Antioxidant and anticholinergic properties of olivetol

Olivetol is a pioneer in diverse syntheses of tetrahydrocannabinol. It is produced by a type of insects, which is used as a pheromone, antiseptic, or repellent agent. In this study, we evaluated the antioxidant properties of olivetol using various methods including Fe3+-Fe2+ reducing, Cu2+-Cu+ reducing, Fe3+-TPTZ reducing, DPPH center dot scavenging, ABTS(center dot+) scavenging, DMPD center dot+ scavenging, superoxide radical scavenging, and Fe2+ chelating effects. The IC50 values of olivetol in the DPPH center dot, ABTS(center dot+), DMPD center dot+, O-2(center dot-), and metal chelating assays were 17.77, 1.94, 19.25, 53.30, and 2.83 mu g/mL, respectively. In this paper, olivetol showed excellent inhibitory effects against human (h) carbonic anhydrase (CA) isoforms I and II (hCA I and II), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes. Both hCA isoenzymes were purified by sepharose-4B-L-tyrosine sulfanilamide affinity chromatography from fresh human blood erythrocytes. Olivetol demonstrated K-i values of 88.0511.15 nM against hCA I, 178.27 +/- 35.94 nM against hCA II, 3.40 +/- 0.34 nM against AChE and 2.73 +/- 0.18 nM against BChE, respectively

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

Natural products from food and plant sources have been used for medicinal usage for ages. Also, natural products with therapeutic significance are compounds derived from animals, plants, or any microorganism. In this study, chrysin, carvacrol, hesperidin, zingerone, and naringin as natural phenols showed excellent inhibitory effects against human (h) carbonic anhydrase (CA) isoforms I and II (hCA I and II), -glucosidase (-Gly), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). These phenolic compounds were tested for the inhibition of -glycosidase, hCA I, hCA II, AChE, and BChE enzymes and demonstrated efficient inhibition profiles with K-i values in the range of 3.70 +/- 0.92-79.66 +/- 20.81nM against hCA I, 2.98 +/- 0.33-84.88 +/- 40.32nM against hCA II, 4.93 +/- 2.01-593.60 +/- 134.74nM against -Gly, 0.52 +/- 0.18-46.80 +/- 17.15nM against AChE, and 1.25 +/- 0.22-32.08 +/- 2.68 against BChE