2,5-bis(4,7-dihydroxy-8-methyl-2-oxo-2H-chromen-3-yl)cyclohexa-2,5-diene-1,4-dione | 1257393-34-2

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 香豆素及其衍生物
• 英文名称: 2,5-bis(4,7-dihydroxy-8-methyl-2-oxo-2H-chromen-3-yl)cyclohexa-2,5-diene-1,4-dione
• 英文别名: 2,3-bis(4,7-dihydroxy-8-methyl-2-oxo-2H-chromen-3-yl)cyclohexa-2,5-diene-1,4-dione；2,3-Bis(4,7-dihydroxy-8-methyl-2-oxochromen-3-yl)cyclohexa-2,5-diene-1,4-dione
• CAS: 1257393-34-2
• 化学式: C₂₆H₁₆O₁₀
• 分子量: 488.407
• InChiKey: SDGVFMJGAULPDK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  36
• 可旋转键数：
  2
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  168
• 氢给体数：
  4
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  2,6-二羟基甲苯 在 zinc(II) chloride 、 三氯氧磷 作用下， 以 水 、 丙酮 为溶剂， 反应 22.0h， 生成 2,5-bis(4,7-dihydroxy-8-methyl-2-oxo-2H-chromen-3-yl)cyclohexa-2,5-diene-1,4-dione
  参考文献：
  名称：

  Hydroxycoumarin Derivatives: Novel and Potent α-Glucosidase Inhibitors

  摘要：

  A novel class of hydroxycoumarin derivatives were found to be potent alpha-glucosidase inhibitors. Their syntheses were reported and the structure-activity relationship was established. Kinetic enzymatic assays indicated that compound 10 was a slow-binding and noncompetitive inhibitor with a K-i value of 589 nM, while compound 11 was a competitive inhibitor with a K-i value of 4.810 mu M. Among all hydroxycoumarin derivatives studied, compounds 10 and 11 exhibited the highest activities, were specific inhibitors of alpha-glucosidase, and could be exploited as the lead compounds for the development of potent alpha-glucosidase inhibitors. Compounds 10 and 11 were also selected for further discussion for the mechanism of enzymatic inhibition.

  DOI：

  10.1021/jm100757r

文献信息

• Hydroxycoumarin Derivatives: Novel and Potent α-Glucosidase Inhibitors
  作者：Qiong Shen、Jialiang Shao、Quan Peng、Wanjin Zhang、Lin Ma、Albert S. C. Chan、Lianquan Gu

  DOI：10.1021/jm100757r

  日期：2010.12.9

  A novel class of hydroxycoumarin derivatives were found to be potent alpha-glucosidase inhibitors. Their syntheses were reported and the structure-activity relationship was established. Kinetic enzymatic assays indicated that compound 10 was a slow-binding and noncompetitive inhibitor with a K-i value of 589 nM, while compound 11 was a competitive inhibitor with a K-i value of 4.810 mu M. Among all hydroxycoumarin derivatives studied, compounds 10 and 11 exhibited the highest activities, were specific inhibitors of alpha-glucosidase, and could be exploited as the lead compounds for the development of potent alpha-glucosidase inhibitors. Compounds 10 and 11 were also selected for further discussion for the mechanism of enzymatic inhibition.