食品科学 ›› 2024, Vol. 45 ›› Issue (8): 37-44.doi: 10.7506/spkx1002-6630-20230530-281

• 基础研究 • 上一篇    下一篇

芦荟大黄素对α-葡萄糖苷酶的抑制机理及其与阿卡波糖的协同作用

秦朝凤,李姣,郝经文,卜雅琴,李胜,陈乃东   

  1. (1.安徽中医药大学药学院,安徽 合肥 230012;2.皖西学院生物与制药工程学院,安徽 六安 237012;3.中药质量评价与品质提升安徽省重点实验室,安徽 六安 237012)
  • 出版日期:2024-04-25 发布日期:2024-05-01
  • 基金资助:
    安徽省中药质量评价与品质提升科研创新团队(2022AH010090); 安徽省级高校自然科学研究重点项目(2022AH051676); 安徽省中药资源保护与持续利用工程实验室重点科技攻关项目(TCMRPSU-2022-06)

Inhibitory Mechanism of Aloe Emodin on α-Glucosidase and Synergistic Effect with Acarbose

QIN Chaofeng, LI Jiao, HAO Jingwen, BU Yaqin, LI Sheng, CHEN Naidong   

  1. (1. College of Pharmacy, Anhui University of Chinese Medicine, Hefei 230012, China;2. College of Biological and Pharmaceutical Engineering, West Anhui University, Lu’an 237012, China;3. Anhui Province Key Laboratory for Quality Evaluation and Improvement of Traditional Chinese Medicine, Lu’an 237012, China)
  • Online:2024-04-25 Published:2024-05-01

摘要: 为探讨芦荟大黄素与α-葡萄糖苷酶的相互作用,本实验采用酶抑制动力学、紫外光谱、红外光谱、荧光光谱等多种光谱分析法研究芦荟大黄素对α-葡萄糖苷酶的抑制机理,并研究芦荟大黄素与阿卡波糖联用的协同效应。结果显示,相较于阿卡波糖,芦荟大黄素具有更好的α-葡萄糖苷酶抑制效果,属于非竞争性和反竞争性的混合型抑制剂。紫外光谱结果表明芦荟大黄素与α-葡萄糖苷酶之间通过相互作用形成了新的复合物。红外光谱中酰胺基团的特征振动结果表明随着芦荟大黄素加入,α-葡萄糖苷酶结构构象发生变化。荧光猝灭实验结果说明,芦荟大黄素是以静态猝灭的方式猝灭α-葡萄糖苷酶的内源性荧光。此外,芦荟大黄素和阿卡波糖联用对α-葡萄糖苷酶活性有一定的协同抑制效果。本研究揭示了芦荟大黄素对α-葡萄糖苷酶的抑制作用机制,为未来将芦荟大黄素作为调节人体血糖的保健食品配方提供了实验依据。

关键词: 芦荟大黄素;α-葡萄糖苷酶;抑制机理;协同抑制;光谱分析

Abstract: In order to investigate the interaction between aloe emodin and α-glucosidase, enzyme kinetics, ultraviolet (UV) spectroscopy, infrared (IR) spectroscopy and fluorescence spectroscopy were employed to investigate the inhibitory mechanism of aloe emodin on α-glucosidase and the synergistic effect of aloe emodin in combination with acarbose was also investigated in this study. The results showed that aloe emodin had better inhibitory effect on α-glucosidase as both a non-competitive and anti-competitive inhibitor when compared with acarbose. The results of UV spectroscopy indicated that a new complex was formed through the interaction between aloe emodin and α-glucosidase. The characteristic vibrations of amide groups in the IR spectra indicated that the structural conformation of α-glucosidase changed with the addition of aloe emodin. The results of fluorescence quenching experiments showed that the endogenous fluorescence of α-glucosidase was statically quenched by aloe emodin. In addition, it was also found that aloe emodin combined with acarbose had a synergistic inhibitory effect on α-glucosidase activity. This study provides an experimental basis for the future application of aloe emodin in health foods for regulating blood glucose.

Key words: aloe emodin; α-glucosidase; inhibitory mechanism; synergistic inhibition; spectral analysis

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