樟树果实花色苷的α-葡萄糖苷酶抑制作用：通过体外和计算机模拟研究的抑制动力学和机理见解。,International Journal of Biological Macromolecules

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樟树果实花色苷的α-葡萄糖苷酶抑制作用：通过体外和计算机模拟研究的抑制动力学和机理见解。
International Journal of Biological Macromolecules ( IF 7.7 ) Pub Date : 2019-09-12 , DOI: 10.1016/j.ijbiomac.2019.09.091
Ji-Guang Chen ₁ , Shao-Fu Wu ₂ , Qing-Feng Zhang ₂ , Zhong-Ping Yin ₂ , Lu Zhang ₃

Affiliation

在2型糖尿病的治疗中，α-葡萄糖苷酶抑制剂被广泛用于抑制餐后血糖。本研究评估了樟脑果实中三种主要色素成分，即花青素，花青素3-芸香苷和花青素-3-O-葡糖苷的体外α-葡糖苷酶抑制活性。我们发现花青素对α-葡糖苷酶具有很强的抑制活性，IC50为5.293×10-3 mM，而花青素3-芸苔苷和花青素-3-O-葡糖苷对α-葡糖苷酶没有抑制活性。矢车菊酯的抑制活性强于阿卡波糖（IC50 1.644 mM），阿卡波糖是目前最常用的餐后血糖治疗药物。动力学分析表明花青素通过竞争抑制α-葡萄糖苷酶，Ki值为0.0183 mM。荧光光谱滴定显示花青素和α-葡萄糖苷酶之间只有一个结合位点，并计算了结合常数。此外，进行分子对接以模拟花青素和α-葡萄糖苷酶之间的结合相互作用。发现Cyanidin通过π-π堆栈相互作用和氢键与α-葡萄糖苷酶催化位点附近的几个残基相互作用。花青素和酶复合物的计算结合能为-105.031 kJ / mol。分子模拟和计算表明范德华力在α-葡萄糖苷酶和花青素的结合中起着至关重要的作用。发现Cyanidin通过π-π堆栈相互作用和氢键与α-葡萄糖苷酶催化位点附近的几个残基相互作用。花青素和酶复合物的计算结合能为-105.031 kJ / mol。分子模拟和计算表明范德华力在α-葡萄糖苷酶和花青素的结合中起着至关重要的作用。发现Cyanidin通过π-π堆栈相互作用和氢键与α-葡萄糖苷酶催化位点附近的几个残基相互作用。花青素和酶复合物的计算结合能为-105.031 kJ / mol。分子模拟和计算表明范德华力在α-葡萄糖苷酶和花青素的结合中起着至关重要的作用。

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α-Glucosidase inhibitory effect of anthocyanins from Cinnamomum camphora fruit: Inhibition kinetics and mechanistic insights through in vitro and in silico studies.

α-Glucosidase inhibitors are widely used to suppress postprandial glycemia in the treatment of type 2 diabetes mellitus. The present study evaluated the in vitro α-glucosidase inhibitory activity of three major pigment constituents of Cinnamomum camphora fruit, namely cyanidin, cyanidin 3-rutinoside, and cyanidin-3-O-glucoside. We found that cyanidin exerted strong inhibitory activity on α-glucosidase, with IC50 of 5.293 × 10-3 mM, whereas cyanidin 3-rutinoside and cyanidin-3-O-glucoside did not show inhibitory activity on α-glucosidase. The inhibitory activity of cyanidin was stronger than that of acarbose (IC50 1.644 mM), the current most commonly used drug for postprandial glycemia. Kinetic analysis indicated that cyanidin inhibited α-glucosidase through competition, with a Ki value of 0.0183 mM. Fluorescence spectrum titration showed only one binding site between cyanidin and α-glucosidase, and the binding constant was calculated. Further, molecular docking was conducted to simulate the binding interactions between cyanidin and α-glucosidase. Cyanidin was found to interact with several residues close to the catalytic site of α-glucosidase through π-π stack interaction and hydrogen bonds. The calculated binding energy of the cyanidin and enzyme complex was -105.031 kJ/mol. Molecular simulation and calculation showed that the van der Waals force played an essential role in the binding of α-glucosidase and cyanidin.

更新日期：2019-09-13

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