|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
All derivatives 4-18 with their intermediates 1-3, were evaluated for in vitro α-glucosidase and α-amylase enzyme inhibition.
|
31451297 |
2020 |
|
Enzyme inhibition disorder
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
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).
|
30571956 |
2019 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
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.
|
29807519 |
2019 |
|
Enzyme inhibition disorder
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
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>).
|
30614298 |
2019 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
All compounds showed a significant enzyme inhibition toward α-glucosidase with IC<sub>50</sub>s of 7.6-25.4 μM.
|
31480857 |
2019 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
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.
|
31514061 |
2019 |
|
Enzyme inhibition disorder
|
0.100 |
GeneticVariation
|
phenotype |
BEFREE |
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.
|
31154083 |
2019 |
|
Enzyme inhibition disorder
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
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.
|
31600541 |
2019 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Natural flavonoid α-glucosidase inhibitors from Retama raetam: Enzyme inhibition and molecular docking reveal important interactions with the enzyme active site.
|
30954838 |
2019 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The α-amylase and α-glucosidase enzyme inhibition, interference with advanced glycation end-products (AGE) formation, and metal chelating abilities were studied.
|
31461832 |
2019 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Furthermore, for the practical applicability of synthesized compound 5, the in vitro acetylcholinesterase as well as α-glucosidase inhibition activities were performed and found moderate enzyme inhibition potential comparable with that of reference inhibitors.
|
29332593 |
2018 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Enzyme inhibition profiles were detected by the UV detector at 415 nm based on the reaction of α-glucosidase and p-nitrophenyl α-d-glucopyranoside (PNPG).
|
29744906 |
2018 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Compounds <b>1</b>⁻<b>3</b> showed potent mixed-type enzyme inhibition against protein tyrosine phosphatase 1B (PTP1B) and α-glucosidase.
|
29786669 |
2018 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Enzyme Inhibition: α-Glucosidase Inhibition was investigated.
|
29165092 |
2018 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Initially, the crude extract of RWL-1 was assessed for potential biological effects of enzyme inhibition and cytotoxicity and was found to exhibit a broad spectrum inhibition for α-glucosidase (37 ± 0.09%) and urease (49.4 ± 0.53%).
|
29304029 |
2018 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The enzyme inhibition bioassay indicated that Compounds 1 and 2 exhibited remarkable inhibitory rate against α-glucosidase and urease, with an IC<sub>50</sub> value of 61.80 ± 5.7, 75.68 ± 6.2 and 74.25 ± 4.3, 190.5 ± 10.31 µg/g, respectively.
|
30167726 |
2018 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
To the best of knowledge, this is the first report of the propanone substituted indole ring containing compounds by in vitro α-glucosidase enzyme inhibition.
|
29807208 |
2018 |
|
Enzyme inhibition disorder
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
To measure enzyme inhibition, 5 μL of the enzyme, 20 μL of substrate and samples were used and for evaluation mode of inhibition, constant amounts of α-glucosidase were incubated with rising concentrations of substrate (PNPG).
|
28367665 |
2017 |
|
Enzyme inhibition disorder
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
The biological studies involved antidiabetic activity i.e. enzyme inhibition of α-amylase and α-glucosidase, Calf Thymus - DNA (CT-DNA) interaction and molecular docking.
|
28892754 |
2017 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Both complexes showed strong enzyme inhibition, i.e., 70% and 90% for α-glucosidase with IC50 = 34.6 and 30.1 μM for 1 and 2, respectively, where acarbose was employed as control.
|
28621397 |
2017 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Compound <b>1</b> showed low to moderate α-glucosidase and urease enzyme inhibition, respectively, and moderate anti-lipid peroxidation activities.
|
28106757 |
2017 |
|
Enzyme inhibition disorder
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The in vitro enzyme inhibition assay was carried out to determine the IC<sub>50</sub> value against α-glucosidase and α-amylase, in silico molecular docking was performed against both enzymes with PyRx tool and simulations were performed using GROMACS tool.
|
28552107 |
2017 |