Inhibitory kinetics and mechanism of oleanolic acid on α-glucosidase

Xie, Zhike; He, Ming; Zhai, Yuhan; Xin, Feifei; Yu, Shu‐Yan; Yu, Shaoxuan; Xiao, Haifang; Song, Yuanda

doi:10.1007/s11694-021-00920-y

Cited by 11 publications

(4 citation statements)

References 45 publications

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“…Therefore, the binding of PEFP and PEBP to α-GLU could inhibit the endogenous fluorescence of the enzyme. 35 This result was consistent with the IC 50 conclusion for α-GLU.…”

Section: Fluorescence Quenching Analysissupporting

confidence: 89%

Inhibitory activities and mechanisms of free and bound phenolics on α-glucosidase in fresh fruits of Phyllanthus emblica Linn. using spectroscopy and molecular docking

Xing,

Xie,

Zeng

et al. 2024

Food Funct.

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“…Therefore, the binding of PEFP and PEBP to α-GLU could inhibit the endogenous fluorescence of the enzyme. 35 This result was consistent with the IC 50 conclusion for α-GLU.…”

Section: Fluorescence Quenching Analysissupporting

confidence: 89%

Inhibitory activities and mechanisms of free and bound phenolics on α-glucosidase in fresh fruits of Phyllanthus emblica Linn. using spectroscopy and molecular docking

Xing,

Xie,

Zeng

et al. 2024

Food Funct.

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“…These results further confirmed that 4,4-dimethylsterols bound to α-glucosidase and rearranged the secondary structure of the latter, which is indicative of a decrease in the functional behavior of α-glucosidase. The addition of 4,4-dimethylsterols induced a decreased α-helix percentage and an increased β-sheet percentage, which were similar to those of other α-glucosidase inhibitors, e.g., vanillin and oleanolic acid. , …”

Section: Results and Discussionsupporting

confidence: 68%

“…The addition of 4,4-dimethylsterols induced a decreased α-helix percentage and an increased β-sheet percentage, which were similar to those of other α-glucosidase inhibitors, e.g., vanillin and oleanolic acid. 48,49 Molecular Docking. Molecular docking has broad applications as a complementary means to understand further structure−activity relationships between proteins and small molecules.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Insights into an α-Glucosidase Inhibitory Profile of 4,4-Dimethylsterols by Multispectral Techniques and Molecular Docking

Xie

Karrar

Zheng

et al. 2021

J. Agric. Food Chem.

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Inhibition of α-glucosidase activity is closely related to the treatment of type 2 diabetes. However, the potential mechanism by which 4,4-dimethylsterols inhibit α-glucosidase has not been elucidated. In this work, the inhibitory activity and mechanism of 4,4-dimethylsterols against α-glucosidase were studied through kinetic analysis, fluorescence spectroscopy, ultraviolet spectroscopy, circular dichroism, and molecular docking. 4,4-Dimethylsterols showed higher inhibition activity against α-glucosidase than acarbose with an IC50 value of 0.71 mg/mL and a noncompetitive inhibition type. They could bind to α-glucosidase through van der Waals forces and hydrogen bonds and quench its endofluorescence with a static quenching mechanism. Changes in the secondary structure of α-glucosidase were induced by its binding interaction with 4,4-dimethylsterols. Molecular docking further indicated that a hydrogen bond was generated between OH at the C-3 position of 4,4-dimethylsterols and the α-glucosidase residue Arg-442. This study provides new insights into the potential utilization of 4,4-dimethylsterols as antidiabetic phytochemicals in dietary supplements.

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“…3(e)) showed that the straight lines in the system intersected at the origin, and the slopes were negatively correlated with the FMBE concentration, indicating that FMBE-induced inhibition was reversible. 56 Figure 3(f) shows Lineweaver-Burk plots for the inhibitory type of FMBE on ⊍-glucosidase. All the straight lines intersected in the third quadrant.…”

Section: Particle Size Distributionmentioning

confidence: 99%

Fermentation of millet bran with Bacillus natto: enhancement of bioactivity levels and the bioactivity of bran extract

Zhang,

Wang,

et al. 2024

J Sci Food Agric

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BackgroundMillet bran (MB), a byproduct of millet production, is rich in functional components, but has a low utilization rate. In recent years, researchers have shown that fermentation can improve the biological activities of cereals and their byproducts. This study used Bacillus natto to ferment millet bran to improve its added value and broaden the application areas of MB. The bioactive component content, physicochemical properties, and functional activities of millet bran extract (MBE) from fermented millet bran were determined.ResultsAfter fermentation, the contents of soluble dietary fiber (SDF), β‐glucan, polypeptides, polyphenols, flavones, and total amino acids increased by 92.0%, 164.4%, 111.4%, 32.5%, 16.4%, and 95.4%, respectively. Scanning electron microscopy revealed that the microscopic morphology of MBE changed from complete and dense blocks to loosely porous shapes after fermentation. After fermentation, the solubility, water holding capacity, and viscosity significantly increased, and the particle size decreased. Moreover, the glucose adsorption capacity (2.1 mmol/g), glucose dialysis retardation index (75.3%), and α‐glucosidase inhibitory (71.4%, mixed reversible inhibition) activity of the fermented MBE (FMBE) were greater than those of the unfermented MBE (0.99 mmol/g, 32.1%, and 35.1%, respectively). FMBE presented better cholesterol and sodium cholate (SC) adsorption properties, and the adsorption was considered inhomogeneous surface adsorption.ConclusionFermentation increased the bioactive component content and improved the physicochemical properties of MBE, thereby improving its hypoglycemic and hypolipidemic properties. This study will not only resolve the problem of millet bran waste but also promote the development of a higher value‐added application method for millet bran.This article is protected by copyright. All rights reserved.

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Inhibitory kinetics and mechanism of oleanolic acid on α-glucosidase

Cited by 11 publications

References 45 publications

Inhibitory activities and mechanisms of free and bound phenolics on α-glucosidase in fresh fruits of Phyllanthus emblica Linn. using spectroscopy and molecular docking

Inhibitory activities and mechanisms of free and bound phenolics on α-glucosidase in fresh fruits of Phyllanthus emblica Linn. using spectroscopy and molecular docking

Insights into an α-Glucosidase Inhibitory Profile of 4,4-Dimethylsterols by Multispectral Techniques and Molecular Docking

Fermentation of millet bran with Bacillus natto: enhancement of bioactivity levels and the bioactivity of bran extract

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