Fujian Provincial Key Laboratory of Innovative Drug Target, School of Pharmaceutical Sciences, Xiamen University, Xiamen 361102, People's Republic of China.
Food Funct. 2022 Mar 7;13(5):2857-2864. doi: 10.1039/d1fo03347f.
Two undescribed phenolic glycosides, trochinenols B and C (1 and2), together with four known analogues (3-6), were isolated from the functional tea Bunge and their α-glucosidase inhibitory kinetics and mechanisms were investigated. It was found that 1 inhibited α-glucosidase in a noncompetitive manner with an IC value of 25.96 μM, while 3 showed a notable inhibitory effect against α-glucosidase in an uncompetitive manner with an IC value of 3.14 μM. Analysis of synchronous fluorescence and circular dichroism spectroscopy indicated that the binding of 1 to α-glucosidase led to the rearrangement and conformational alteration of the α-glucosidase enzyme. Furthermore, molecular docking indicated that 1 had a high affinity close to the active site pocket of α-glucosidase and indirectly inhibited the catalytic activity of the enzyme. However, 3 was bound to the entrance part of the active center of α-glucosidase and could hinder the release of the substrate as well as the catalytic reaction product, eventually suppressing the catalytic activity of α-glucosidase.
从功能茶（Bunge）中分离得到两个未被描述的酚糖苷，即 trochinenols B 和 C（1 和 2），以及四个已知的类似物（3-6），并研究了它们对α-葡萄糖苷酶的抑制动力学和机制。结果表明，1 以非竞争性方式抑制α-葡萄糖苷酶，IC 值为 25.96 μM，而 3 以显著的竞争性方式抑制α-葡萄糖苷酶，IC 值为 3.14 μM。同步荧光和圆二色性光谱分析表明，1 与α-葡萄糖苷酶结合导致酶的重排和构象改变。此外，分子对接表明 1 与α-葡萄糖苷酶的活性口袋具有很高的亲和力，从而间接抑制了酶的催化活性。然而，3 与α-葡萄糖苷酶的活性中心入口部分结合，能够阻碍底物和催化反应产物的释放，最终抑制α-葡萄糖苷酶的催化活性。
