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- W4312182231 abstract "Pepsin plays an important role in nutrient metabolism. Apigenin (AP) is a beneficial polyphenol to human health. To enhance the bioavailability of AP and elucidate the inhibitory effect of AP on pepsin, the interaction mechanism of AP with pepsin was investigated using spectroscopic analysis and molecular docking, and the activity of pepsin and antioxidant activity of AP was also evaluated. Specifically, AP performed static quenching of pepsin and had only one binding site on pepsin. More interestingly, the interaction between AP and pepsin was spontaneous, while hydrogen bonds and van der Waals forces were the main binding forces. Generally, synchronous and three-dimensional fluorescence confirmed that AP induced the conformational changes of pepsin, and molecular docking proved the above results and illustrated the specific binding patterns. Specifically, AP inhibited the activity of pepsin, while pepsin decreased the antioxidant activity of AP. These results provided useful information for elucidating the interactions between AP and pepsin." @default.
- W4312182231 created "2023-01-04" @default.
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- W4312182231 date "2022-12-01" @default.
- W4312182231 modified "2023-10-16" @default.
- W4312182231 title "Exploration of binding mechanism of apigenin to pepsin: spectroscopic analysis, molecular docking, enzyme activity and antioxidant assays" @default.
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- W4312182231 doi "https://doi.org/10.1016/j.saa.2022.122281" @default.
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