(S)-1,3-dichloro-6-(pyrrolidine-1-carbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one | 1055393-08-2

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (S)-1,3-dichloro-6-(pyrrolidine-1-carbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
• CAS: 1055393-08-2
• 化学式: C₁₂H₁₃Cl₂N₃O₂
• 分子量: 302.16
• InChiKey: VNRILDVYGIYMBV-QMMMGPOBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.66
• 重原子数：
  19.0
• 可旋转键数：
  1.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  55.2
• 氢给体数：
  0.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  2-萘甲醇 、 (S)-1,3-dichloro-6-(pyrrolidine-1-carbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one 在 potassium carbonate 作用下， 生成 (S)-1-chloro-3-(naphthalen-2-ylmethoxy)-6-(pyrrolidine-1-carbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
  参考文献：
  名称：

  Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP)

  摘要：

  We report the synthesis and in vitro activity of a series of novel pyrrolidinyl pyridones and pyrazinones as potent inhibitors of prolyl oligopeptidase (POP). Within this series, compound 39 was co-crystallized within the catalytic site of a human chimeric POP protein which provided a more detailed understanding of how these inhibitors interacted with the key residues within the catalytic pocket.

  DOI：

  10.1016/j.bmcl.2008.06.067
• 作为产物：
  描述：

  四氢吡咯 、 (6S)-1,3-dichloro-4-oxo-7,8-dihydro-6H-pyrrolo[1,2-a]pyrazine-6-carboxylic acid 在 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 (S)-1,3-dichloro-6-(pyrrolidine-1-carbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
  参考文献：
  名称：

  Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP)

  摘要：

  We report the synthesis and in vitro activity of a series of novel pyrrolidinyl pyridones and pyrazinones as potent inhibitors of prolyl oligopeptidase (POP). Within this series, compound 39 was co-crystallized within the catalytic site of a human chimeric POP protein which provided a more detailed understanding of how these inhibitors interacted with the key residues within the catalytic pocket.

  DOI：

  10.1016/j.bmcl.2008.06.067