| Title : Exploring the binding effects and inhibiting mechanism of hyperoside to lipase using multi-spectroscopic approaches, isothermal titration calorimetry, inhibition kinetics and molecular dynamics - Zeng_2023_RSC.Adv_13_6507 |
| Author(s) : Zeng Z , Wu D , Tang L , Hu X , Zhang J , Geng F |
| Ref : RSC Adv , 13 :6507 , 2023 |
| Abstract : Hyperoside (HYP) is a flavonoid with various physiological activities. The present study examined the interaction mechanism between HYP and lipase using multi-spectrum and computer-aided techniques. Results demonstrated that the force type of HYP on lipase was mainly hydrogen bond, hydrophobic interaction force, and van der Waals force, and HYP had an excellent binding affinity with lipase at 1.576 x 10(5) M(-1). HYP dose-dependently inhibited lipase in the inhibition experiment, and its IC(50) value was 1.92 x 10(-3) M. Moreover, the results suggested that HYP could inhibit the activity by binding to essential groups. Conformational studies indicated that the conformation and microenvironment of lipase were slightly changed after the addition of HYP. Computational simulations further confirmed the structural relationships of HYP to lipase. The interaction between HYP and lipase can provide ideas for the development of functional foods related to weight loss. The results of this study help comprehend the pathological significance of HYP in biological systems, as well as its mechanism. |
| ESTHER : Zeng_2023_RSC.Adv_13_6507 |
| PubMedSearch : Zeng_2023_RSC.Adv_13_6507 |
| PubMedID: 36845588 |
Zeng Z, Wu D, Tang L, Hu X, Zhang J, Geng F (2023)
Exploring the binding effects and inhibiting mechanism of hyperoside to lipase using multi-spectroscopic approaches, isothermal titration calorimetry, inhibition kinetics and molecular dynamics
RSC Adv
13 :6507
Zeng Z, Wu D, Tang L, Hu X, Zhang J, Geng F (2023)
RSC Adv
13 :6507