3α-hydroxy-11-oxo-18α-olean-12-en-30-oic acid | 118492-17-4

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: 3α-hydroxy-11-oxo-18α-olean-12-en-30-oic acid
• 英文别名: (2S,4aS,6aR,6aS,6bR,8aR,10R,12aS,14bS)-10-hydroxy-2,4a,6a,6b,9,9,12a-heptamethyl-13-oxo-3,4,5,6,6a,7,8,8a,10,11,12,14b-dodecahydro-1H-picene-2-carboxylic acid
• CAS: 118492-17-4
• 化学式: C₃₀H₄₆O₄
• 分子量: 470.693
• InChiKey: MPDGHEJMBKOTSU-CMZPMQISSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.4
• 重原子数：
  34
• 可旋转键数：
  1
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.87
• 拓扑面积：
  74.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  3-Desoxy-2.3-didehydro-18α-glycyrrhetinsaeuremethylester 在 偶氮二异丁腈 、 氢溴酸 、 三正丁基氢锡 、 间氯过氧苯甲酸 、 lithium iodide 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 苯 为溶剂， 反应 6.5h， 生成 3α-hydroxy-11-oxo-18α-olean-12-en-30-oic acid
  参考文献：
  名称：

  Glycyrrhetinic acid derivatives as potent inhibitors of Na+, K+-ATPase. Synthesis and structure-activity relationships

  摘要：

  A series of ring A-modified GA derivatives (26 compounds) has been systematically synthesized and the structure-activity relationship investigated for inhibition of canine kidney Na+, K+-ATPase in vitro. The most potent inhibitory activity was found with a group of the 3-deoxygenated derivatives including 5, 6, 9, 10 and 11. The high inhibition may be closely related to the hydrophobic character of the A-ring of these compounds. This finding suggests that the ATP-binding site at the active center of the enzyme is located in a hydrophobic environment.

  DOI：

  10.1016/0223-5234(92)90147-s

文献信息

• Glycyrrhetinic acid derivatives as potent inhibitors of Na+, K+-ATPase. Synthesis and structure-activity relationships
  作者：T Terasawa、T Okada、T Hara、K Itoh

  DOI：10.1016/0223-5234(92)90147-s

  日期：1992.6

  A series of ring A-modified GA derivatives (26 compounds) has been systematically synthesized and the structure-activity relationship investigated for inhibition of canine kidney Na+, K+-ATPase in vitro. The most potent inhibitory activity was found with a group of the 3-deoxygenated derivatives including 5, 6, 9, 10 and 11. The high inhibition may be closely related to the hydrophobic character of the A-ring of these compounds. This finding suggests that the ATP-binding site at the active center of the enzyme is located in a hydrophobic environment.