2,5-bis(tert-butoxycarbonyl)-2,3,4,5-tetrahydro-1H-pyrido[4,3-b]indole-8-carboxylic acid | 1512863-59-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: 2,5-bis(tert-butoxycarbonyl)-2,3,4,5-tetrahydro-1H-pyrido[4,3-b]indole-8-carboxylic acid
• CAS: 1512863-59-0
• 化学式: C₂₂H₂₈N₂O₆
• 分子量: 416.474
• InChiKey: UWYPZWGBGUQOAX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.42
• 重原子数：
  30.0
• 可旋转键数：
  1.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  98.07
• 氢给体数：
  1.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  2,5-bis(tert-butoxycarbonyl)-2,3,4,5-tetrahydro-1H-pyrido[4,3-b]indole-8-carboxylic acid 在 叠氮磷酸二苯酯 、 sodium hydride 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 、 甲苯 、 mineral oil 为溶剂， 反应 5.5h， 生成 di-tert-butyl 8-(methyl((2-(trimethylsilyl)ethoxy)carbonyl)amino)-3,4-dihydro-1H-pyrido[4,3-b]indole-2,5-dicarboxylate
  参考文献：
  名称：

  Targeting Low-Druggability Bromodomains: Fragment Based Screening and Inhibitor Design against the BAZ2B Bromodomain

  摘要：

  Bromodomains are epigenetic reader domains that have recently become popular targets. In contrast to BET bromodomains, which have proven druggable, bromodomains from other regions of the phylogenetic tree have shallower pockets. We describe successful targeting of the challenging BAZ2B bromodomain using biophysical fragment screening and structure-based optimization of high ligand-efficiency fragments into a novel series of low-micromolar inhibitors. Our results provide attractive leads for development of BAZ2B chemical probes and indicate the whole family may be tractable.

  DOI：

  10.1021/jm401582c
• 作为产物：
  描述：

  4-羧基苯肼盐酸盐 在 盐酸 、 4-二甲氨基吡啶 、 sodium hydroxide 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 甲醇 、 水 为溶剂， 反应 6.0h， 生成 2,5-bis(tert-butoxycarbonyl)-2,3,4,5-tetrahydro-1H-pyrido[4,3-b]indole-8-carboxylic acid
  参考文献：
  名称：

  Targeting Low-Druggability Bromodomains: Fragment Based Screening and Inhibitor Design against the BAZ2B Bromodomain

  摘要：

  Bromodomains are epigenetic reader domains that have recently become popular targets. In contrast to BET bromodomains, which have proven druggable, bromodomains from other regions of the phylogenetic tree have shallower pockets. We describe successful targeting of the challenging BAZ2B bromodomain using biophysical fragment screening and structure-based optimization of high ligand-efficiency fragments into a novel series of low-micromolar inhibitors. Our results provide attractive leads for development of BAZ2B chemical probes and indicate the whole family may be tractable.

  DOI：

  10.1021/jm401582c