A series of ureas derived from phenethylamines were synthesized and evaluated for human carbonic anhydrase (hCA) I and II, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzyme inhibitory activities and antioxidant properties. The ureas were synthesized from the reactions of substituted phenethylamines with N,N-dimethylcarbamoyl chloride; then, the synthesized compounds were converted to their corresponding phenolic derivatives via O-demethylation. hCA I and II were effectively inhibited by the newly synthesized compounds, with K values in the range of 0.307-0.432 nM for hCA I and 0.149-0.278 nM for hCA II. On the other hand, the K parameters of these compounds for AChE and BChE were determined in the range of 0.129-0.434 and 0.095-0.207 nM, respectively. Phenolic ureas also showed good antioxidant activities.

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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 Fe 31 2Fe 21 reducing, Cu 21 2Cu 1 reducing, Fe 31 2TPTZ reducing, DPPH scavenging, ABTS 1 scavenging, DMPD 1 scavenging, superoxide radical scavenging, and Fe 21 chelating effects. The IC 50 values of olivetol in the DPPH , ABTS 1 , DMPD 1 , O 2 2 , and metal chelating assays were 17.77, 1.94, 19.25, 53.30, and 2.83 lg/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 88.05 6 11.15 nM against hCA I, 178.27 6 35.94 nM against hCA II, 3.40 6 0.34 nM against AChE and 2.73 6 0.18 nM against BChE, respectively.

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), α-glucosidase (α-Gly), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). These phenolic compounds were tested for the inhibition of α-glycosidase, hCA I, hCA II, AChE, and BChE enzymes and demonstrated efficient inhibition profiles with K values in the range of 3.70 ± 0.92-79.66 ± 20.81 nM against hCA I, 2.98 ± 0.33-84.88 ± 40.32 nM against hCA II, 4.93 ± 2.01-593.60 ± 134.74 nM against α-Gly, 0.52 ± 0.18-46.80 ± 17.15 nM against AChE, and 1.25 ± 0.22-32.08 ± 2.68 against BChE.

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In this paper, synephrine and phenylephrine compounds showed excellent inhibitory effects against human carbonic anhydrase (hCA) isoforms I and II, α-amylase, α-glycosidase, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). Synephrine and phenylephrine had K values of 199.02 ± 16.01 and 65.01 ± 5.00 μM against hCA I and 336.02 ± 74.01 and 92.04  ±  18.03 μM against hCA II, respectively. On the other hand, their K values were found to be 169.10  ±  80.03 and 88.03  ±  5.01 nM against AChE and 177.06  ±  6.01 and 78.03  ±  3.05 nM against BChE, respectively. α-Amylase and α-glycosidase enzymes were easily inhibited by these compounds. α-Glycosidase inhibitors, generally defined to as starch blockers, are anti-diabetic drugs that help to decrease post comestible blood glucose levels.