Antioxidant, α-Glucosidase Inhibitory Activity and Molecular Docking Study of Gallic Acid, Quercetin and Rutin: A Comparative Study

Limanto, Agus; Simamora, Adelina; Santoso, Adit Widodo; Timotius, Kris Herawan

doi:10.21705/mcbs.v3i2.60

Cited by 29 publications

(30 citation statements)

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“…It was shown that the docked conformation (pink line) and the crystal structure conformation (yellow line) of acarbose overlapped well, and the root mean square deviation (RMSD) of the overlap was 0.75 Å, which proved the reliability and reasonability of box parameter settings in docking ( Figure S2). Furthermore, many investigations confirmed that GA was shown to be a competitive inhibitor on α-glucosidase, similar to that found for acarbose, suggesting that GA and acarbose bound with α-glucosidase at similar binding sites in a manner that prevented substrate binding [32][33][34]. Based on the confirmed statements previously reported, we defined the box using the binding site of acarbose as a reference during docking.…”

Section: Molecular Dockingsupporting

confidence: 66%

Characterizations and Assays of α-Glucosidase Inhibition Activity on Gallic Acid Cocrystals: Can the Cocrystals be Defined as a New Chemical Entity During Binding with the α-Glucosidase?

Xue

Jia

et al. 2020

Molecules

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Cocrystallization with co-former (CCF) has proved to be a powerful approach to improve the solubility and even bioavailability of poorly water-soluble active pharmaceutical ingredients (APIs). However, it is still uncertain whether a cocrystal would exert the pharmacological activity in the form of a new chemical entity, an API-CCF supramolecule. In the present study, gallic acid (GA)-glutaric acid and GA-succinimide cocrystals were screened. The solubility, dissolution rate and oral bioavailability of the two cocrystals were evaluated. As expected, AUCs of GA-glutaric acid and GA-succinimide cocrystals were 1.86-fold and 2.60-fold higher than that of single GA, respectively. Moreover, experimental evaluations on α-glucosidase inhibition activity in vitro and theoretical simulations were used to detect whether the two cocrystals would be recognized as a new chemical entity during binding with α-glucosidase, a target protein in hypoglycemic mechanisms. The enzyme activity evaluation results showed that both GA and glutaric acid displayed α-glucosidase inhibition activity, and GA-glutaric acid cocrystals showed strengthened α-glucosidase inhibition activity at a moderate concentration, which is attributed to synergism of the two components. Molecular docking displayed that the GA-glutaric acid complex deeply entered the active cavity of the α-glucosidase in the form of a supramolecule, which made the guest-enzyme binding configuration more stable. For the GA and succinimide system, succinimide showed no enzyme inhibition activity, however, the GA-succinimide complex presented slightly higher α-glucosidase inhibition activity than that of GA. Molecular docking simulation indicated that the guest molecules entering the active cavity of the α-glucosidase were free GA and succinimide, not the GA-succinimide supramolecule.

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Section: Molecular Dockingsupporting

confidence: 66%

Characterizations and Assays of α-Glucosidase Inhibition Activity on Gallic Acid Cocrystals: Can the Cocrystals be Defined as a New Chemical Entity During Binding with the α-Glucosidase?

Xue

Jia

et al. 2020

Molecules

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“…Because the cavity of the site is large enough to accommodate polysaccharides, the authors supposed that sm molecules cannot bind as well in the active site as larger molecules, as rutin, being than quercetin, could demonstrate [46]. These two cases also revealed that querceti different inhibitory modes with a noncompetitive inhibition of α-amylase vs a compe inhibition of α-glucosidase [10,46]. The results showed effective inhibition of intestinal α-glucosidase by both (−)-catechin and gallic acid, whereas thymoquinone was not active under the evaluated concentration range (data not shown).…”

Section: Mechanism and Ic 50 Determinationsmentioning

confidence: 99%

Linking the Phytochemicals and the α-Glucosidase and α-Amylase Enzyme Inhibitory Effects of Nigella sativa Seed Extracts

Tiji

Bouhrim

Addi

et al. 2021

Foods

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Nigella sativa L. (Ranunculaceae), commonly referred to as black seeds or black cumin, is used in popular medicine (herbal) all over the world for the treatment and prevention of several diseases, including diabetes. This study aims to investigate the inhibitory effect of N. sativa extracts and fractions against the activities of intestinal α-glucosidase and pancreatic α-amylase in vitro, and to explain the inhibitory effect of these fractions against these enzymes by identifying their active compounds responsible for this effect and determine their modes of inhibition. To do so, N. sativa hexane and acetone extracts were prepared and analyzed by GC–MS and HPLC–DAD, respectively. The hexane extract was further fractioned into eight different fractions, while the acetone extract generated eleven fractions. The extracts as well as the resulting fractions were characterized and evaluated for their potential in vitro antidiabetic activity using intestinal α-glucosidase and pancreatic α-amylase inhibitory assays in vitro. Hexane extract and fractions were less active than acetone extract and fractions. In the case of intestinal α-glucosidase activity, the acetone fraction SA3 had a high inhibitory effect on intestinal α-glucosidase activity with 72.26 ± 1.42%, comparable to the effect of acarbose (70.90 ± 1.12%). For the pancreatic α-amylase enzymatic inhibitory assay, the acetone fractions showed an inhibitory capacity close to that for acarbose. In particular, the SA2 fraction had an inhibitory effect of 67.70 ± 0.58% and was rich in apigenin and gallic acid. From these fractions, apigenin, (−)-catechin, and gallic acid were further characterized for their inhibitory actions. IC50 and inhibition mode were determined by analyzing enzyme kinetic parameters and by molecular modeling. Interestingly, (−)-catechin showed a possible synergistic effect with acarbose toward α-glucosidase enzyme inhibition, whereas apigenin showed an additive effect with acarbose toward α-amylase enzymatic inhibition. Furthermore, we studied the toxicity of N. sativa hexane and acetone extracts as well as that of acetone fractions. The result of acute toxicity evaluation demonstrated that N. sativa extracts were nontoxic up to a concentration of 10 g/kg, except for fraction SA3. Taken together, these results indicate that N. sativa extracts and/or derived compounds could constitute promising nutraceuticals for the prevention and treatment of type 2 diabetes mellitus.

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“…reptans leaves on α-glucosidase. Various phenolic and flavonoid compounds have been reported to inhibit αglucosidase in vitro (Limanto et al, 2019;Yin et al, 2014).…”

Section: In Vitro Antidiabetic Activitymentioning

confidence: 99%

Antioxidant, Antidiabetic, and Anti-obesity Potential of Ipomoea reptans Poir Leaves

et al. 2020

Self Cite

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Ipomoea reptans Poir or kangkung is a popular leafy vegetable, a favorite to people in Asian countries. However, limited information is available on their bioactivities. In the present study, the antioxidant, antidiabetic, and anti-obesity potential of I. reptans leaves were investigated. Different fractions (ethanol, ethyl acetate, and hexane) of I. reptans leaves were evaluated for their scavenging activity on DPPH radicals, whereas their reducing potential was investigated by cupric reducing antioxidant capacity (CuPRAC), total antioxidant, and reducing power assays. The antidiabetic potential was investigated by their inhibition effect on a-glucosidase. Total phenolic and flavonoid contents of I. reptans leaves were solvent dependent. Ethyl acetate contained the highest phenolic content, followed by ethanol and hexane fractions. However, for flavonoid content, the order was ethanol > ethyl acetate > hexane. All fractions showed DPPH scavenging activity in a concentration-dependent manner, with activities weaker than standards ascorbic acid and BHT, in the order of ethanol > ethyl acetate > hexane. All fractions showed reducing capacity, but only hexane and ethanol fractions of I. reptans leaves showed inhibition on a-glucosidase, with hexane showed more potent inhibition compared to acarbose. The study also found that fractions of I. reptans inhibit lipase and trypsin, enzymes related to lipid metabolism. Findings in this study offer a prospect for I. reptans leaves as a functional food source for antioxidant, antidiabetic, and anti-obesity purposes.

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Antioxidant, α-Glucosidase Inhibitory Activity and Molecular Docking Study of Gallic Acid, Quercetin and Rutin: A Comparative Study

Cited by 29 publications

References 0 publications

Characterizations and Assays of α-Glucosidase Inhibition Activity on Gallic Acid Cocrystals: Can the Cocrystals be Defined as a New Chemical Entity During Binding with the α-Glucosidase?

Characterizations and Assays of α-Glucosidase Inhibition Activity on Gallic Acid Cocrystals: Can the Cocrystals be Defined as a New Chemical Entity During Binding with the α-Glucosidase?

Linking the Phytochemicals and the α-Glucosidase and α-Amylase Enzyme Inhibitory Effects of Nigella sativa Seed Extracts

Antioxidant, Antidiabetic, and Anti-obesity Potential of Ipomoea reptans Poir Leaves

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