2-(3-(4-phenyl-1H-imidazol-1-yl)propyl)isoindoline-1,3-dione | 1048983-26-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: 2-(3-(4-phenyl-1H-imidazol-1-yl)propyl)isoindoline-1,3-dione
• CAS: 1048983-26-1
• 化学式: C₂₀H₁₇N₃O₂
• 分子量: 331.374
• InChiKey: BTGOXHIXHQHUAM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.24
• 重原子数：
  25.0
• 可旋转键数：
  5.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.15
• 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-(3-(4-phenyl-1H-imidazol-1-yl)propyl)isoindoline-1,3-dione 在 一水合肼 作用下， 以 乙醇 为溶剂， 反应 5.0h， 以67%的产率得到3-(4-苯基咪唑-1-基)丙烷-1-胺
  参考文献：
  名称：

  Structure Based Development of Phenylimidazole-Derived Inhibitors of Indoleamine 2,3-Dioxygenase

  摘要：

  Indoleamine 2,3-dioxygenase (IDO) is emerging as an important new therapeutic target for the treatment of cancer, chronic viral infections, and other diseases characterized by pathological immune suppression. With the goal of developing more potent IDO inhibitors, a systematic study of 4-phenylimidazole (4-PI) derivatives was undertaken. Computational docking experiments guided design and synthesis efforts with analogues of 4-PI. In particular, three interactions of 4-PI analogues with IDO were studied: the active site entrance, the interior of the active site, and the heme iron binding. The three most potent inhibitors (1, 17, and 18) appear to exploit interactions with C129 and S167 in the interior of the active site. All three inhibitors are approximately 10-fold more potent than 4-PI. The study represents the first example of enzyme inhibitor development with the recently reported crystal structure of IDO and offers important lessons in the search for more potent inhibitors.

  DOI：

  10.1021/jm800512z
• 作为产物：
  描述：

  N-(3-溴丙基)苯二胺 、 4-苯基咪唑 在 sodium hydride 作用下， 以 四氢呋喃 为溶剂， 反应 3.5h， 以57%的产率得到2-(3-(4-phenyl-1H-imidazol-1-yl)propyl)isoindoline-1,3-dione
  参考文献：
  名称：

  Structure Based Development of Phenylimidazole-Derived Inhibitors of Indoleamine 2,3-Dioxygenase

  摘要：

  Indoleamine 2,3-dioxygenase (IDO) is emerging as an important new therapeutic target for the treatment of cancer, chronic viral infections, and other diseases characterized by pathological immune suppression. With the goal of developing more potent IDO inhibitors, a systematic study of 4-phenylimidazole (4-PI) derivatives was undertaken. Computational docking experiments guided design and synthesis efforts with analogues of 4-PI. In particular, three interactions of 4-PI analogues with IDO were studied: the active site entrance, the interior of the active site, and the heme iron binding. The three most potent inhibitors (1, 17, and 18) appear to exploit interactions with C129 and S167 in the interior of the active site. All three inhibitors are approximately 10-fold more potent than 4-PI. The study represents the first example of enzyme inhibitor development with the recently reported crystal structure of IDO and offers important lessons in the search for more potent inhibitors.

  DOI：

  10.1021/jm800512z