Rb2 inhibits α-glucosidase and regulates glucose metabolism by activating AMPK pathways in HepG2 cells

Antidiabetic potential: in vitro inhibition effects of some natural phenolic compounds on α‐glycosidase and α‐amylase enzymes

“…IC 50 values of phenolic compounds and standard (acarbose) compounds exhibited the following order: CAPE (29.01 nM) ≈ Curcumin (29.31 nM) ≤ Rosmarinic acid (32.53 nM) < Olivetol (45.47 nM) < Tetrakis (64.64 nM) < Isoliquiritigenin (68.61 nM) < Resveratrol (99.18 nM) < p‐Coumaric acid (157.96 nM) < Acarbose (22.80 μM). The results clearly showed that all natural phenolic compounds demonstrated effective α‐glycosidase inhibitory effects than that of acarbose (22.80 μM) as standard AGI. However, the most effective IC 50 values were recorded by CAPE and curcumin with K i values of 29.01 and 29.31 nM, respectively.…”

“…Inhibition of α‐amylase enzyme that plays an important role in digestion of glycogen and starch is evaluated as strategy for the therapy of disturbances in carbohydrate uptake, such as obesity and diabetes, as well as, periodontal diseases and dental caries . For α‐amylase, natural phenolic compounds had IC 50 values in the range of 137.36–737.23 nM.…”

Inhibition profiles of Voriconazole against acetylcholinesterase, α‐glycosidase, and human carbonic anhydrase I and II isoenzymes

“…For this enzyme, Voriconazole had an IC 50 value of 40.77nM, R 2 of 0.9846, and K i value of 17.47 ± 1.51 nM (Table and Figures ). IC 50 values of Voriconazole and standard (acarbose) compound exhibited the following order: Voriconazole (40.77nM; R 2 : 0.9846) < acarbose (22800 nM) . On the other hand, K i values of Voriconazole and standard (acarbose) compound exhibited the following order: Voriconazole (17.47 ± 1.51 nM) < acarbose (12600 ± 780 nM) …”

Synthesis, characterization, antioxidant, antidiabetic, anticholinergic, and antiepileptic properties of novel N‐substituted tetrahydropyrimidines based on phenylthiourea

“…These results clearly indicated that newly synthesized compounds as well as future similar derivatives may function as drugs for the treatment of AD. For the ?‐glycosidase enzyme, the novel N‐substituted tetrahydropyrimidines based on phenylthiourea ( 1a‐d ) had IC 50 values in the range of 56.18 to 70.31 nM and K i values in the range of 48.95 ± 11.00 to 91.03 ± 9.21 nM (Table and Figure ). The results obviously showed that all these novel derivatives (1a‐d) demonstrated efficient ?‐glycosidase inhibitory effects than that of acarbose (IC 50 : 22.8 M) as standard ?‐glycosidase inhibitor. However, the most effective K i values were obtained by 1‐(4‐(2‐hydroxyphenyl)‐6‐methyl‐1‐phenyl‐2‐thioxo‐1,2,3,4‐tetrahydropyrimidin‐5‐yl) ethanone ( 1a ) and methyl‐3‐(4‐hydroxybutyl)‐4‐(2‐hydroxyphenyl)‐6‐methyl‐1‐phenyl‐2‐thioxo‐1,2,3,4‐tetrahydropyrimidine‐5‐carboxylate ( 1d ), with K i values of 48.95 ± 11.00 and 52.47 ± 8.43 nM, respectively. Reducing capability of novel N‐substituted tetrahydropyrimidines based on phenylthiourea ( 1a‐d ) was evaluated by reduction of Fe([CN] 6 ) 3 to Fe([CN] 6 ) 2 .…”