Insight into interaction mechanism between theaflavin‐3‐gallate and α‐glucosidase using spectroscopy and molecular docking analysis

Liu, Siyuan; Yin, Lin; Yi, Ju-Zhen; Zhang, Liming; Yang, Liqun

doi:10.1111/jfbc.13550

Cited by 19 publications

(6 citation statements)

References 59 publications

(97 reference statements)

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“…The synchronous fluorescence spectra of CYP2D6 are measured at Δ λ = 15 and 60 nm, respectively [46]. As shown in Figure 6a(1),b(1), with the increase of quercetin/hyperoside, the emission fluorescence intensity of CYP2D6 at Δ λ = 15 nm decreases regularly with a slight blue shift, indicating that hydrophobicity near Tyr increases.…”

Section: Resultsmentioning

confidence: 99%

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: Resultsmentioning

confidence: 99%

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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“…The interactions of some flavonoids and triterpenoid saponins with better affinity values are shown in Figures 6 and 7. The binding site on α-glucosidase by flavonoids 1, 2, 3, 8 was similar to that of acarbose [57]. They were stabilized at the active site of α-glucosidase and interacted with amino acid residues by hydrogen bonds, salt bridge, hydrophobic interaction and other types of forces, via residues, such as His280, Asp325, Asp307, Arg315, Leu313, Pro312, Thr310, Ser311, Asp242, Glu332 and Ala281.…”

Section: Interaction Between α-Glucosidase and Components In Quinoa H...mentioning

confidence: 88%

Screening for α-Glucosidase-Inhibiting Saponins from Pressurized Hot Water Extracts of Quinoa Husks

Shi

et al. 2022

Foods

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The present study extracted total saponins from quinoa husks with pressurized hot water extraction and optimized the extraction conditions. The response surface methodology (RSM) with a Box–Behnken design (BBD) was employed to investigate the effects of extraction flow rate, extraction temperature and extraction time on the extraction yield of total saponins. A maximal yield of 23.06 mg/g was obtained at conditions of 2 mL/min, 210 °C and 50 min. The constituents of the extracts were analyzed by liquid chromatography–mass spectrometry (LC-MS). A total of twenty-three compounds were identified, including five flavonoids, seventeen triterpenoid saponins and a phenolic acid. Moreover, we performed an in vitro assay for the α-glucosidase activity and found a stronger inhibitory effect of the quinoa husk extracts than acarbose, suggesting its potential to be developed into functional products with hypoglycemic effect. Finally, our molecular docking analyses indicated triterpenoid saponins as the main bioactive components.

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“…By referring to the studies related to the inhibition assay of theaflavin-3-gallate and combining the results of the preexperiment, the concentration range of the four theaflavins was finalized to be 0-60 μg mL −1 (with a final concentration of 0-0.76 μM). 18 MMP-2 inhibition experiments were conducted in accordance with Rathee's method, with slight modifications. 19 Succinyl gelatin served as the substrate to assess the inhibitory activity of the four theaflavins against MMP-2.…”

Section: Assay Of Mmp-2 Inhibition Activitymentioning

confidence: 99%

Inhibition mechanism of theaflavins on matrix metalloproteinase-2: inhibition kinetics, multispectral analysis, molecular docking and molecular dynamics simulation

Guo,

Hu,

Yang

et al. 2024

Food Funct.

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Insight into interaction mechanism between theaflavin‐3‐gallate and α‐glucosidase using spectroscopy and molecular docking analysis

Cited by 19 publications

References 59 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

Screening for α-Glucosidase-Inhibiting Saponins from Pressurized Hot Water Extracts of Quinoa Husks

Inhibition mechanism of theaflavins on matrix metalloproteinase-2: inhibition kinetics, multispectral analysis, molecular docking and molecular dynamics simulation

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