2-amino-N-(1-benzylpiperidin-4-yl)-5-fluorobenzamide

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 哌啶类
• 英文名称: 2-amino-N-(1-benzylpiperidin-4-yl)-5-fluorobenzamide
• 化学式: C₁₉H₂₂FN₃O
• 分子量: 327.402
• InChiKey: BEHUQIHCMJMUDC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  24
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.315
• 拓扑面积：
  58.4
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-amino-N-(1-benzylpiperidin-4-yl)-5-fluorobenzamide 在 氢气 、 palladium(II) hydroxide 、 sodium hydride 、 potassium carbonate 、 溶剂黄146 、 potassium iodide 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 20.0 ℃ 、101.33 kPa 条件下， 反应 18.5h， 生成 1-(cyclopentylmethyl)-6-fluoro-2-(2-fluorophenyl)-3-(1-(3-(2-phenyl-1H-imidazol-1-yl)propyl) piperidin-4-yl)-2,3-dihydroquinazolin-4(1H)-one
  参考文献：
  名称：

  Discovery of Novel KRAS-PDEδ Inhibitors by Fragment-Based Drug Design

  摘要：

  [Graphics]Targeting KRAS-PDE delta protein-protein interactions with small molecules represents a promising opportunity for developing novel antitumor agents. However, current KRAS-PDE delta inhibitors are limited by poor cellular antitumor potency and the druggability of the target remains to be validated by new inhibitors. To tackle these challenges, herein, novel, highly potent KRAS-PDE delta inhibitors were identified by fragment-based drug design, providing promising lead compounds or chemical probes for investigating the biological functions and druggability of KRAS-PDE delta interaction.

  DOI：

  10.1021/acs.jmedchem.8b00057
• 作为产物：
  描述：

  4-氨基-1-苄基哌啶 、 2-氨基-5-氟苯甲酸 在 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 12.0h， 生成 2-amino-N-(1-benzylpiperidin-4-yl)-5-fluorobenzamide
  参考文献：
  名称：

  Discovery of Novel KRAS-PDEδ Inhibitors by Fragment-Based Drug Design

  摘要：

  [Graphics]Targeting KRAS-PDE delta protein-protein interactions with small molecules represents a promising opportunity for developing novel antitumor agents. However, current KRAS-PDE delta inhibitors are limited by poor cellular antitumor potency and the druggability of the target remains to be validated by new inhibitors. To tackle these challenges, herein, novel, highly potent KRAS-PDE delta inhibitors were identified by fragment-based drug design, providing promising lead compounds or chemical probes for investigating the biological functions and druggability of KRAS-PDE delta interaction.

  DOI：

  10.1021/acs.jmedchem.8b00057