Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia

Wu, Xia-Qing; Ding, Huafang; Hu, Xiaofeng; Pan, Junhui; Liao, Yijing; Gong, Deming; Zhang, Guowen

doi:10.1016/j.jff.2018.07.022

Cited by 93 publications

(58 citation statements)

References 39 publications

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“…Another study found that the binding sites of apigenin were Ser311 and Gly309 Journal of Food Quality [26]. Gallocatechin gallate was reported to form hydrogen bonds with Arg 315 and Phe 303 to effectively inhibit the catalytic activity of α-glucosidase [27]. ose different results also obviously suggested that the structures of phenolic compounds may profoundly affect their binding sites on α-glucosidase.…”

Section: Molecular Docking Results Of Pancreatic Lipase and α-Glucosimentioning

confidence: 99%

Digestive Enzyme Inhibition of Different Phenolic Fractions and Main Phenolic Compounds of Ultra-High-Pressure-Treated Palm Fruits: Interaction and Molecular Docking Analyses

Zhou

Liu

et al. 2020

Journal of Food Quality

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The purpose of the present work was to evaluate the inhibitory effects of different phenolic extracts from non- and ultra-high-pressure- (UHP-) treated palm fruits and their main phenolic compounds against pancreatic lipase and α-glucosidase and to further analyze the interaction and inhibitory mechanisms of two main phenolics (caffeic acid and catechin). Results showed that the free, esterified, and insoluble-bound phenolic fractions from the non- and UHP-treated fruits demonstrated good inhibitory effects towards two enzymes. The insoluble-bound phenolic fraction, regardless of UHP treatment, presented the strongest inhibitory capacities, and UHP treatment significantly upgraded the inhibitory effects of these phenolic fractions (lipase IC50 : 78.01 vs. 72.50 μg/mL; α-glucosidase IC50 : 76.42 vs. 64.51 μg/mL). Catechin and caffeic acid, main phenolic compounds detected in all phenolic fractions of the fruits, showed similar efficiencies on inhibiting the two enzymes, which were consistent with the findings observed by molecular docking analysis. Moreover, these two phenolic compounds exhibited a synergy effect on inhibiting pancreatic lipase and α-glucosidase at a relatively high combination concentration with the ratio of 1 : 1. Therefore, the present work may be helpful for further application of palm fruits as food supplements or nutraceuticals to control energy intake to improving some chronic metabolic diseases.

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Section: Molecular Docking Results Of Pancreatic Lipase and α-Glucosimentioning

confidence: 99%

Digestive Enzyme Inhibition of Different Phenolic Fractions and Main Phenolic Compounds of Ultra-High-Pressure-Treated Palm Fruits: Interaction and Molecular Docking Analyses

Zhou

Liu

et al. 2020

Journal of Food Quality

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“…The IC 50 values of isorhamnetin 3- O -rutinoside and rutin were 90.19 ± 3.27 μg/mL and 126.86 ± 8.58 μg/mL, respectively. Previous studies about the α-glucosidase inhibition of various phenolics have also been studied, and the results also indicated that the α-glucosidase inhibitory capacity was closely dependent on the phenolic standard [46,47]. Han et al [46] pointed out that phloretin reversibly inhibited α-glucosidase in a mixed-type manner, with an IC 50 value of 31.26 μg/mL.…”

Section: Resultsmentioning

confidence: 99%

Phenolic Composition, Antioxidant Properties, and Inhibition toward Digestive Enzymes with Molecular Docking Analysis of Different Fractions from Prinsepia utilis Royle Fruits

Zhang

Jia

et al. 2018

Molecules

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The present study investigated the phenolic profiles and antioxidant properties of different fractions from Prinsepia utilis Royle fruits using molecular docking analysis to delineate their inhibition toward digestive enzymes. A total of 20 phenolics was identified and quantified. Rutin, quercetin-3-O-glucoside, and isorhamnetin-3-O-rutinoside were the major phenolic compounds in the total phenolic fraction and flavonoid-rich fraction. The anthocyanin-rich fraction mainly contained cyanidin-3-O-glucoside and cyanidin-3-O-rutinoside. All of the fractions exhibited strong radical scavenging activities and good inhibition on cellular reactive oxygen species (ROS) generation in H2O2-induced HepG2 cells, as evaluated by DPPH and 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) assays. Moreover, the powerful inhibitory effects of those fractions against pancreatic lipase and α-glucosidase were observed. The major phenolic compounds that were found in the three fractions also showed good digestive enzyme inhibitory activities in a dose-dependent manner. Molecular docking analysis revealed the underlying inhibition mechanisms of those phenolic standards against digestive enzymes, and the theoretical analysis data were consistent with the experimental results.

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“…The binding constant K a and the number of binding sites n of the interaction between the quencher and the biomacromolecule during the static quenching process were calculated with Eqn (6)

\log \frac{F_{0} - F}{F} = n \log K_{normala} - n \log \frac{1}{[Q_{t}] - \frac{((), F_{0} - F) ([], P_{normalt})}{F_{0}}}

[ P t ] and [ Q t ] represent the concentrations of α ‐glucosidase and CRA in the system, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…The binding constant K a and the number of binding sites n of the interaction between the quencher and the biomacromolecule during the static quenching process were calculated with Eqn (6). 43 log…”

Section: Thermodynamic Parametersmentioning

confidence: 99%

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

Pan

et al. 2019

J Sci Food Agric

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BACKGROUND The suppression of α‐glucosidase activity to retard glucose absorption is an important therapy for type‐2 diabetes. Corosolic acid (CRA) is a potential antidiabetic component in many plant‐based foods and herbs. In this study, the interplay mechanism between α‐glucosidase and corosolic acid was investigated by several methods, including three‐dimensional fluorescence spectra, circular dichroism spectra, and molecular simulation. RESULTS Corosolic acid significantly inhibited α‐glucosidase reversibly in an uncompetitive manner and its IC50 value was 1.35 × 10−5 mol L−1. A combination of CRA with myricetin exerted a weak synergy against α‐glucosidase. The intrinsic fluorescence of α‐glucosidase was quenched via a static quenching course and the binding constant was 3.47 × 103 L mol−1 at 298 K. The binding of CRA to α‐glucosidase was mainly driven by hydrophobic forces and resulted in a partial extension of the protein polypeptide chain with a loss of α‐helix content. The molecular simulation illustrated that CRA bound to the entrance part of the active center of α‐glucosidase and interacted with the amino acid residues Ser157, Arg442, Phe303, Arg315, Tyr158, and Gln353, which could hinder the release of substrate and catalytic reaction product, eventually suppressing the catalytic activity of α‐glucosidase. CONCLUSIONS These results may suggest new insights into corosolic acid from food sources as a potential α‐glucosidase inhibitor that could better control diabetes. © 2019 Society of Chemical Industry

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Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia

Cited by 93 publications

References 39 publications

Digestive Enzyme Inhibition of Different Phenolic Fractions and Main Phenolic Compounds of Ultra-High-Pressure-Treated Palm Fruits: Interaction and Molecular Docking Analyses

Digestive Enzyme Inhibition of Different Phenolic Fractions and Main Phenolic Compounds of Ultra-High-Pressure-Treated Palm Fruits: Interaction and Molecular Docking Analyses

Phenolic Composition, Antioxidant Properties, and Inhibition toward Digestive Enzymes with Molecular Docking Analysis of Different Fractions from Prinsepia utilis Royle Fruits

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

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