Essential oils from the inflorescence of Cymbopogon schoenanthus and C. nervatus growing in Northern Sudan were examined for their chemical composition, antiproliferative activity against human breast carcinoma and human colon adenocarcinoma cell lines, antioxidant activity (phosphomolybdenum, antiradical, reducing power, and ferrous chelating), and enzyme inhibition activity against acetylcholinesterase butyrylcholinesterase, tyrosinase, α-glucosidase, and α-amylase.
The disecosteroid displayed moderate carbolytic enzyme inhibition activity as distinguished by its inhibitive effects against α-amylase and α-glucosidase (IC<sub>50</sub> 0.40 and 0.54 mg/mL, respectively).
The disecosteroid displayed moderate carbolytic enzyme inhibition activity as distinguished by its inhibitive effects against α-amylase and α-glucosidase (IC<sub>50</sub> 0.40 and 0.54 mg/mL, respectively).
Kinetic study of enzyme inhibition indicated that the most potent compound, 6e, is a non-competitive inhibitor of α-glucosidase with a Ki value of 72 µM.
Results showed that ZLA (2, 5 mg/kg; i.p.) treatment significantly ameliorated the Cu(II)-induced impairment of hippocampus-dependent learning and memory, whereas rivastigmine, an AChE inhibitor showing a similar potency of enzyme inhibition to ZLA, had no obvious effect.
Further, these results were validated based on enzyme inhibition assays where OMC demonstrated enzyme inhibitory activity towards α-amylase (IC<sub>50</sub> 3.4 mg mL<sup>-1</sup>) and α-glucosidase (IC<sub>50</sub> 38.49 μg mL<sup>-1</sup>).
Kinetics of enzyme inhibition revealed a mixed-type inhibition of eeAChE activity by HPH whereas F7 acted through an uncompetitive mode; in contrast inhibition of human AChE by HPH and F7 was uncompetitive.
Natural flavonoid α-glucosidase inhibitors from Retama raetam: Enzyme inhibition and molecular docking reveal important interactions with the enzyme active site.
Total bioactive contents, antioxidant (phosphomolybdenum and metal chelating, DPPH, ABTS, FRAP and CUPRAC) and enzyme inhibition (cholinesterases, tyrosinase α-amylase, and α-glucosidase) potential were assessed utilizing in vitro bioassays.
The synthesized heterocyclic hybrids 7a-j were evaluated for their in vitro acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitory activities, therein compounds 7h and 7j displayed more potent AChE and BChE enzyme inhibition than the standard drug with IC<sub>50</sub> values of 3.22, 2.01, 12.40 and 10.45 mM, respectively.
The use of bioactivity screening method combined with preparation method of bioactive compounds and an in vitro enzyme inhibition assay facilitated the efficient screening and isolation of the cyclooxygenase-2 inhibitors from complex samples.
Further, these results were validated based on enzyme inhibition assays where OMC demonstrated enzyme inhibitory activity towards α-amylase (IC<sub>50</sub> 3.4 mg mL<sup>-1</sup>) and α-glucosidase (IC<sub>50</sub> 38.49 μg mL<sup>-1</sup>).
The enzyme inhibition mode was also studied and the kinetic studies revealed that the synthetic molecules have shown competitive mode of inhibition against α-amylase and non-competitive mode of inhibition against α-glucosidase enzyme.
Phytochemical content, antioxidant activity, and enzyme inhibition effect of Salvia eriophora Boiss. & Kotschy against acetylcholinesterase, α-amylase, butyrylcholinesterase, and α-glycosidase enzymes.
All sulfonamide derivatives studied here can be considered as good candidates to develop novel CAs or AChE inhibitor candidates based on the enzyme inhibition potencies with their low cytotoxicity and tumor selectivity.
Although the majority of research focuses on its mechanism via cyclooxygenase-2 (COX-2) enzyme inhibition, we identified a distinct mechanism behind celecoxib anti-cancer abilities.
The α-amylase and α-glucosidaseenzyme inhibition, interference with advanced glycation end-products (AGE) formation, and metal chelating abilities were studied.
Total bioactive contents, antioxidant (phosphomolybdenum and metal chelating, DPPH, ABTS, FRAP and CUPRAC) and enzyme inhibition (cholinesterases, tyrosinase α-amylase, and α-glucosidase) potential were assessed utilizing in vitro bioassays.
The isolated metabolites were evaluated for enzyme inhibition activity against α-glucosidase and α-amylase, free radical scavenging activity against DPPH and ABTS radicals, metal chelating and antibacterial activity against clinical pathogens.
Natural flavonoid α-glucosidase inhibitors from Retama raetam: Enzyme inhibition and molecular docking reveal important interactions with the enzyme active site.
The isolated metabolites were evaluated for enzyme inhibition activity against α-glucosidase and α-amylase, free radical scavenging activity against DPPH and ABTS radicals, metal chelating and antibacterial activity against clinical pathogens.