Inhibitory interaction of narcissoside on α-glucosidase from Aspergillus niger and Saccharomyces cerevisiae by spectral analysis and molecular docking

Fan, Yangyang; Tao, Yanzhou; Wang, Haihui; Wang, Meizi; Li, Li

doi:10.1016/j.molstruc.2022.133262

Cited by 10 publications

(4 citation statements)

References 43 publications

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“…Moreover, K a values of CYP2D6-quercetin are much higher than CYP2D6-hyperoside at the same temperature, proving that the stability of CYP2D6-quercetin complex is stronger than CYP2D6hyperoside [38].…”

Section: Molecular Docking and Dynamics Simulationsmentioning

confidence: 91%

Interactions studies of CYP2D6 with quercetin and hyperoside by spectral analysis and molecular dynamics simulations

Wang,

Cui

et al. 2023

Luminescence

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Some ingredients from herbal medicine can significantly affect the activity of CYP2D6, thus leading to serious interactions between herbs and drugs. Quercetin and hyperoside are active ingredients widely found in vegetables, fruits, and herbal medicines. Quercetin and hyperoside have many biological activities. In this work, the characteristic bindings of CYP2D6 with quercetin/hyperoside are revealed by multi‐spectroscopy analysis, molecular docking, and molecular dynamics simulations. The fluorescence of CYP2D6 is statically quenched by quercetin and hyperoside. The Ka values of CYP2D6‐quercetin/hyperoside range from 104 L·mol‐1, which indicates that these two flavonoids bind moderately to CYP2D6. Meanwhile, quercetin has a stronger quenching ability to CYP2D6 than that of hyperoside. The secondary structure of CYP2D6 is obviously changed by binding with quercetin/hyperoside. The docking results reveal that the quercetin/hyperoside enters the active site of CYP2D6 near Heme, and binds to CYP2D6 by hydrogen bonds and van der Waals forces. The molecular dynamics simulation results indicate that the binding of quercetin/hyperoside can stabilize the two complexes, enhance the flexibility of CYP2D6 backbone atoms, and make a more unfolded and looser structure of CYP2D6.

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Section: Molecular Docking and Dynamics Simulationsmentioning

confidence: 91%

Interactions studies of CYP2D6 with quercetin and hyperoside by spectral analysis and molecular dynamics simulations

Wang,

Cui

et al. 2023

Luminescence

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“…In the present study, since the variation range of the temperature was narrow, the enthalpy change (∆H • ) can be considered as a constant [7]. The main non-covalent interactions between the enzymes and inhibitors include electrostatic interaction, hydrophobic forces, hydrogen bonds, and van der Waals forces.…”

Section: Fluorescence Quenching Assaymentioning

confidence: 98%

“…Natural resources, such as traditional herbs and functional fruits, are abundant with biologically interesting compounds, which have been widely explored for the development of naturally occurring inhibitors on α-glucosidase. For example, narcissoside isolated from Anoectochilus roxburghii [7], trilobatin obtained from Lithocarpus polystachyu [8], prenylated flavonoids isolated from mulberry leaves [9], and furanolabdane diterpenoids from the tropical plant Graptophyllum pictum [10] are reported to exhibit an excellent inhibitory effect on α-glucosidase, showing high application potential as natural antidiabetic agents.…”

Section: Introductionmentioning

confidence: 99%

Insight into the Inhibitory Mechanisms of Hesperidin on α-Glucosidase through Kinetics, Fluorescence Quenching, and Molecular Docking Studies

Kaliaperumal,

Zhang,

Gao

et al. 2023

Foods

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The α-glucosidase inhibitor is of interest to researchers due to its association with type-II diabetes treatment by suppressing postprandial hyperglycemia. Hesperidin is a major flavonoid in orange fruit with diverse biological properties. This paper evaluates the effects of hesperidin on α-glucosidase through inhibitory kinetics, fluorescence quenching, and molecular docking methods for the first time. The inhibition kinetic analysis shows that hesperidin reversibly inhibited the α-glucosidase activity with an IC50 value of 18.52 μM and the inhibition was performed in an uncompetitive type. The fluorescence quenching studies indicate that the intrinsic fluorescence of α-glucosidase was quenched via a static quenching process and only one binding site was present between the hesperidin and α-glucosidase. The interaction between them was spontaneous and mainly driven by hydrogen bonds, as well as hydrophobic forces. Furthermore, the molecular docking results suggest that hesperidin might bond to the entrance or outlet part of the active site of α-glucosidase through a network of five hydrogen bonds formed between hesperidin and the four amino acid residues (Trp709, Arg422, Asn424, and Arg467) of α-glucosidase and the hydrophobic effects. These results provide new insight into the inhibitory mechanisms of hesperidin on α-glucosidase, supporting the potential application of a hesperidin-rich orange product as a hypoglycemic functional food.

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“…Meanwhile, AG is an important membrane‐binding enzyme with the function of hydrolyzing glycosidic bonds of disaccharides or polysaccharides that are digested from starch to release monosaccharides, resulting in elevated postprandial blood glucose (Hsieh et al, 2015). Despite being effective medications for lowering postprandial hyperglycemia, long‐term use of acarbose and miglitol may result in particular side effects, such as gastrointestinal discomfort characterized by stomach pain, diarrhea, and flatulence (Şöhretoğlu et al, 2023; Wang, Fan, et al, 2023).…”

Section: Introductionmentioning

confidence: 99%

Discovery of vitexin as a novel α‐glucosidase inhibitors in mulberry (Morus alba L.) by untargeted metabolomics combined with molecular docking: A comprehensive study from mechanism to synergy effects

Wang,

Zhang,

Wang

et al. 2024

eFood

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Mulberry (Morus alba L.) leaf can effectively inhibit the digestion of starchy foods, and α‐glucosidase (AG) is its main target. This study employed an untargeted metabolomics approach combined with molecular docking to identify AG inhibitors. Subsequently, inhibition kinetics, fluorescence spectroscopy, and interaction force analysis were utilized to investigate the inhibitory mechanism. Results indicated that vitexin exhibited significant reversible inhibition of AG through competitive inhibition, with an IC50 value of 105.50 ± 1.30 μg/mL. Molecular docking revealed hydrogen bonding as the main interaction force between vitexin and AG, and quenching mechanism analysis showed that they underwent static quenching driven by entropy. The results of the combined experiment showed that 1‐deoxynojirimycin (DNJ), a known bioactive component in mulberry, has a synergistic effect of inhibiting AG activity with vitexin. This study elucidates the potential mechanism of vitexin in inhibiting AG activity and provides theoretical evidence for utilizing vitexin‐DNJ complexes as functional components of AG inhibitors.

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Inhibitory interaction of narcissoside on α-glucosidase from Aspergillus niger and Saccharomyces cerevisiae by spectral analysis and molecular docking

Cited by 10 publications

References 43 publications

Interactions studies of CYP2D6 with quercetin and hyperoside by spectral analysis and molecular dynamics simulations

Interactions studies of CYP2D6 with quercetin and hyperoside by spectral analysis and molecular dynamics simulations

Insight into the Inhibitory Mechanisms of Hesperidin on α-Glucosidase through Kinetics, Fluorescence Quenching, and Molecular Docking Studies

Discovery of vitexin as a novel α‐glucosidase inhibitors in mulberry (Morus alba L.) by untargeted metabolomics combined with molecular docking: A comprehensive study from mechanism to synergy effects

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