Inhibition Mechanism of Mulberry Prenylated Flavonoids Sanggenone D/Kuwanon G Against α-Glucosidase and the Regulation of Glucose via GLUT4 Pathway
文献类型: 外文期刊
作者: Wu, Erwen 1 ; Zhu, Yanqing 1 ; Wei, Qingyi 2 ; Lu, Huijie 3 ; Zou, Yuxiao 1 ; Liu, Fan 1 ; Li, Qian 1 ;
作者机构: 1.Guangdong Acad Agr Sci, Sericultural & Agrifood Res Inst, Guangdong Key Lab Agr Prod Proc, Key Lab Funct Foods,Minist Agr & Rural Affairs, Guangzhou 510610, Peoples R China
2.South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510640, Peoples R China
3.Guangdong Acad Agr Sci, Inst Anim Sci, Guangzhou 510640, Peoples R China
4.Guangdong Acad Agr Sci, Sericultural & Agrifood Res Inst, Yiheng Rd 133, Guangzhou 510610, Peoples R China
关键词: alpha-glucosidase; inhibition mechanisms; molecular docking; Western blotting; structure-activity relationship
期刊名称:NUTRIENTS ( 影响因子:5.0; 五年影响因子:6.0 )
ISSN:
年卷期: 2025 年 17 卷 9 期
页码:
收录情况: SCI
摘要: Background: Inhibition of alpha-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 alpha-glucosidase were investigated and the hypoglycemic pathways were explored in the current study. Results: The outcomes indicate that sanggenone D (IC50: 4.51 x 10-5 mol/L) and kuwanon G (IC50: 3.83 x 10-5 mol/L) inhibited alpha-glucosidase activity by non-competition/anti-competition mixed inhibition and competitive inhibition, respectively. Moreover, the secondary structure of alpha-glucosidase was altered by static quenching and exhibited a decrease in alpha-helix and beta-antiparallel content, and an increase in beta-sheet content. Furthermore, the interaction forces between sanggenone D/kuwanon G and alpha-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 alpha-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.
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