2-(3-溴苯基)-1,3-苯并恶唑-5-胺 | 293737-81-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 中文名称: 2-(3-溴苯基)-1,3-苯并恶唑-5-胺
• 英文名称: 2-(3-Bromophenyl)-1,3-benzoxazol-5-amine
• CAS: 293737-81-2
• 化学式: C₁₃H₉BrN₂O
• mdl: MFCD00445929
• 分子量: 289.131
• InChiKey: RBEUAXOSGXEKQB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  17
• 可旋转键数：
  1
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  52
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-叔丁氧羰基-L-丙氨酸 、 2-(3-溴苯基)-1,3-苯并恶唑-5-胺 在 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 四氢呋喃 为溶剂， 生成
  参考文献：
  名称：

  Fragment-Based Design of Small Molecule X-Linked Inhibitor of Apoptosis Protein Inhibitors

  摘要：

  We report on a general structure- and NMR-based approach to derive druglike small molecule inhibitors of protein-protein interactions in a rapid and efficient manner. We demonstrate the utility of the approach by deriving novel and effective SMAC mimetics targeting the antiapoptotic protein X-linked inhibitor of apoptosis protein (XIAP). The XIAP baculovirus IAP repeat 3 (Bir3) domain binds directly to the N-terminal of caspase-9, thus inhibiting programmed cell death. It has been shown that in the cell this interaction can be displaced by the protein second mitochondrial activator of caspases (SMAC) and that its N-terminal tetrapeptide region (NH2-AVPI, Ala-Val-Pro-Ile) is responsible for this activity. However, because of their limited cell permeability, synthetic SMAC peptides are inefficient when tested in cultured cells, limiting their use as potential chemical tools or drug candidates against cancer cells. Hence, as an application, we report on the derivation of novel, selective, druglike, cell permeable SMAC mimics with cellular activity.

  DOI：

  10.1021/jm8006992

文献信息

• Fragment-Based Design of Small Molecule X-Linked Inhibitor of Apoptosis Protein Inhibitors
  作者：Jui-Wen Huang、Ziming Zhang、Bainan Wu、Jason F. Cellitti、Xiyun Zhang、Russell Dahl、Chung-Wai Shiau、Kate Welsh、Aras Emdadi、John L. Stebbins、John C. Reed、Maurizio Pellecchia

  DOI：10.1021/jm8006992

  日期：2008.11.27

  We report on a general structure- and NMR-based approach to derive druglike small molecule inhibitors of protein-protein interactions in a rapid and efficient manner. We demonstrate the utility of the approach by deriving novel and effective SMAC mimetics targeting the antiapoptotic protein X-linked inhibitor of apoptosis protein (XIAP). The XIAP baculovirus IAP repeat 3 (Bir3) domain binds directly to the N-terminal of caspase-9, thus inhibiting programmed cell death. It has been shown that in the cell this interaction can be displaced by the protein second mitochondrial activator of caspases (SMAC) and that its N-terminal tetrapeptide region (NH2-AVPI, Ala-Val-Pro-Ile) is responsible for this activity. However, because of their limited cell permeability, synthetic SMAC peptides are inefficient when tested in cultured cells, limiting their use as potential chemical tools or drug candidates against cancer cells. Hence, as an application, we report on the derivation of novel, selective, druglike, cell permeable SMAC mimics with cellular activity.