Erwen Wu
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Erwen Wu has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Fan Liu
Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing; Sericultural & Agri-Food Research Institute, Guangdong Academy of Agricultural Sciences, Guangzhou 510610, China
2 shared publications - Huijie Lu
Institute of Animal Science, Guangdong Academy of Agricultural Sciences, Guangzhou 510640, China
2 shared publications - Qian Li
Guangdong Academy of Agricultural Sciences Ministry of Agriculture and Rural Affairs Guangdong Key Laboratory of Agricultural Products Processing Key Laboratory of Functional Foods Sericultural & Agri-Food Research Institute 510610 Guangzhou China
2 shared publications - Qingyi Wei
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China
2 shared publications - Yanqing Zhu
Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing; Sericultural & Agri-Food Research Institute, Guangdong Academy of Agricultural Sciences, Guangzhou 510610, China
2 shared publications - Yuxiao Zou
Sericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences/Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs/Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, China
2 shared publications
Latest Publications
- Open Access
Inhibition Mechanism of Mulberry Prenylated Flavonoids Sanggenone D/Kuwanon G Against α-Glucosidase and the Regulation of Glucose via GLUT4 Pathway
Background: Inhibition of α-glucosidase activity is recognized as an effective strategy for managing type 2 diabetes. Methods: The inhibitory mechanisms of two kinds of mulberry flavonoids, namely sanggenone D and kuwanon G, on α-glucosidase were investigated and the hypoglycemic pathways were explored in the current study. Results: The outcomes indicate that sanggenone D (IC50: 4.51 × 10−5 mol/L) and kuwanon G (IC50: 3.83 × 10−5 mol/L) inhibited α-glucosidase activity by non-competition/anti-competition mixed inhibition and competitive inhibition, respectively. Moreover, the secondary structure of α-glucosidase was altered by static quenching and exhibited a decrease in α-helix and β-antiparallel content, and an increase in β-sheet content. Furthermore, the interaction forces between sanggenone D/kuwanon G and α-glucosidase were hydrophobic interactions and hydrogen bonds, as evidenced by molecular docking. The binding affinity, stability, and binding energy aligned with the results of IC50. Notably, the cyclization in sanggenone D structure resulted in a decrease in the number of phenolic hydroxyl groups and thus a reduction in the formation of hydrogen bonds, which ultimately diminished the binding affinity of sanggenone D to α-glucosidase. In addition, Western blot analysis further indicated that sanggenone D and kuwanon G regulated glucose metabolism by activating the GLUT4 pathway. Conclusions: The results provided useful reference for the application of sanggenone D and kuwanon G in hypoglycemic functional components.
Open AccessInhibition Mechanism of Mulberry Prenylated Flavonoids Sanggenone D/Kuwanon G Against α-Glucosidase and the Regulation of Glucose via GLUT4 Pathway
Background: Inhibition of α-glucosidase activity is recognized as an effective strategy for managing type 2 diabetes. Methods: The inhibitory mechanisms of two kinds of mulberry flavonoids, namely sanggenone D and kuwanon G, on α-glucosidase were investigated and the hypoglycemic pathways were explored in the current study. Results: The outcomes indicate that sanggenone D (IC50: 4.51 × 10−5 mol/L) and kuwanon G (IC50: 3.83 × 10−5 mol/L) inhibited α-glucosidase activity by non-competition/anti-competition mixed inhibition and competitive inhibition, respectively. Moreover, the secondary structure of α-glucosidase was altered by static quenching and exhibited a decrease in α-helix and β-antiparallel content, and an increase in β-sheet content. Furthermore, the interaction forces between sanggenone D/kuwanon G and α-glucosidase were hydrophobic interactions and hydrogen bonds, as evidenced by molecular docking. The binding affinity, stability, and binding energy aligned with the results of IC50. Notably, the cyclization in sanggenone D structure resulted in a decrease in the number of phenolic hydroxyl groups and thus a reduction in the formation of hydrogen bonds, which ultimately diminished the binding affinity of sanggenone D to α-glucosidase. In addition, Western blot analysis further indicated that sanggenone D and kuwanon G regulated glucose metabolism by activating the GLUT4 pathway. Conclusions: The results provided useful reference for the application of sanggenone D and kuwanon G in hypoglycemic functional components.
- Open Access
- 11 March 2025
- Published by MDPI AG in Preprints.org
Inhibition Mechanism of Sanggenone D/ Kuwanon G Against α-Glucosidase and the Regulation of Glucose via GLUT4 Pathway
Inhibition of α-glucosidase activity is considered to be an effective treatment for type 2 diabetes. The inhibitory mechanisms of sanggenone D and kuwanon G on α-glucosidase were investigated and the pathways for hypoglycemic effects were explored in the current study. The outcomes indicated that sanggenone D (IC50: 4.51 × 10-5 mol/L) and kuwanon G (IC50: 3.83 × 10-5 mol/L) inhibited α-glucosidase activity by non-competition/anti-competition mixed inhibition and competitive inhibition, respectively. Besides, the secondary structure of α-glucosidase were altered by static quenching, and exhibited the decrease in α-helix, β-antiparallel content, while increase in β-sheet content. Furthermore, the interaction forces between sanggenone D/kuwanon G and α-glucosidase were hydrophobic interactions and hydrogen bonds as evidenced by molecular docking. The binding affinity, stability and binding energy aligned with the results of IC50. Cyclization in sanggenone D structure resulted in a decrease in the number of phenolic hydroxyl groups and thus a reduction in the formation of hydrogen bonds, which ultimately diminished the binding affinity of sanggenone D to α-glucosidase. In addition, western blot results showed that sanggenone D and kuwanon G regulated glucose metabolism by activating of GLUT4 pathway.
- 11 March 2025
- Published by MDPI AG in Preprints.org
Open AccessInhibition Mechanism of Sanggenone D/ Kuwanon G Against α-Glucosidase and the Regulation of Glucose via GLUT4 Pathway
Inhibition of α-glucosidase activity is considered to be an effective treatment for type 2 diabetes. The inhibitory mechanisms of sanggenone D and kuwanon G on α-glucosidase were investigated and the pathways for hypoglycemic effects were explored in the current study. The outcomes indicated that sanggenone D (IC50: 4.51 × 10-5 mol/L) and kuwanon G (IC50: 3.83 × 10-5 mol/L) inhibited α-glucosidase activity by non-competition/anti-competition mixed inhibition and competitive inhibition, respectively. Besides, the secondary structure of α-glucosidase were altered by static quenching, and exhibited the decrease in α-helix, β-antiparallel content, while increase in β-sheet content. Furthermore, the interaction forces between sanggenone D/kuwanon G and α-glucosidase were hydrophobic interactions and hydrogen bonds as evidenced by molecular docking. The binding affinity, stability and binding energy aligned with the results of IC50. Cyclization in sanggenone D structure resulted in a decrease in the number of phenolic hydroxyl groups and thus a reduction in the formation of hydrogen bonds, which ultimately diminished the binding affinity of sanggenone D to α-glucosidase. In addition, western blot results showed that sanggenone D and kuwanon G regulated glucose metabolism by activating of GLUT4 pathway.