[(S)-3-(2-Triisopropylsilanyloxy-ethyl)-indan-(1E)-ylidene]-acetic acid ethyl ester | 877400-11-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: [(S)-3-(2-Triisopropylsilanyloxy-ethyl)-indan-(1E)-ylidene]-acetic acid ethyl ester
• CAS: 877400-11-8
• 化学式: C₂₄H₃₈O₃Si
• 分子量: 402.649
• InChiKey: NTFGGYBMYCHZDS-HXUWFJFHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.7
• 重原子数：
  28.0
• 可旋转键数：
  9.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  35.53
• 氢给体数：
  0.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  [(S)-3-(2-Triisopropylsilanyloxy-ethyl)-indan-(1E)-ylidene]-acetic acid ethyl ester 在 palladium on activated charcoal sodium hydroxide 、 ammonium acetate 、 四丁基氟化铵 、 甲酸铵 、 N,N'-羰基二咪唑 作用下， 以 甲醇 为溶剂， 生成 2-[(1R,3S)-3-(2-Hydroxy-ethyl)-indan-1-yl]-acetamide
  参考文献：
  名称：

  Design, synthesis, and biological evaluation of monopyrrolinone-based HIV-1 protease inhibitors possessing augmented P2′ side chains

  摘要：

  A series of monopyrrolinone-based HIV-1 protease inhibitors possessing rationally designed P2' side chains have been synthesized and evaluated for activity against wild-type HIV-1 protease. The most potent inhibitor displays subnanomolar potency in vitro for the wild-type HIV-1 protease. Additionally, the monopyrrolinone inhibitors retain potency in cellular assays against clinically significant mutant forms of the virus. X-ray structures of these inhibitors bound in the wild-type enzyme reveal important insights into the observed biological activity.

  DOI：

  10.1016/j.bmcl.2005.11.011
• 作为产物：
  描述：

  (R)-3-(2-Triisopropylsilanyloxy-ethyl)-indan-1-one 在 双[Α,Α-双(三氟甲基)苯甲醇合]二苯硫 、 硼酸三乙酯 、 锌 作用下， 以 四氢呋喃 为溶剂， 生成 [(S)-3-(2-Triisopropylsilanyloxy-ethyl)-indan-(1E)-ylidene]-acetic acid ethyl ester
  参考文献：
  名称：

  Design, synthesis, and biological evaluation of monopyrrolinone-based HIV-1 protease inhibitors possessing augmented P2′ side chains

  摘要：

  A series of monopyrrolinone-based HIV-1 protease inhibitors possessing rationally designed P2' side chains have been synthesized and evaluated for activity against wild-type HIV-1 protease. The most potent inhibitor displays subnanomolar potency in vitro for the wild-type HIV-1 protease. Additionally, the monopyrrolinone inhibitors retain potency in cellular assays against clinically significant mutant forms of the virus. X-ray structures of these inhibitors bound in the wild-type enzyme reveal important insights into the observed biological activity.

  DOI：

  10.1016/j.bmcl.2005.11.011