5'-bromospiro[1,3-dioxepane-2,3'-1H-indole]-2'-one | 840512-97-2

• 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: 5'-bromospiro[1,3-dioxepane-2,3'-1H-indole]-2'-one
• CAS: 840512-97-2
• 化学式: C₁₂H₁₂BrNO₃
• 分子量: 298.136
• InChiKey: XIUASJJNQFYRAK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  17
• 可旋转键数：
  0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  47.6
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  5'-bromospiro[1,3-dioxepane-2,3'-1H-indole]-2'-one 在 羟胺钾盐 、 四丁基溴化铵 、 potassium carbonate 、 potassium iodide 作用下， 以 甲醇 、 丙酮 为溶剂， 反应 7.5h， 生成 2-(5'-bromo-2'-oxospiro[1,3-dioxepane-2,3'-indole]-1'-yl)-N-hydroxyacetamide
  参考文献：
  名称：

  Novel indoline-2,3-dione derivatives as inhibitors of aminopeptidase N (APN)

  摘要：

  Aminopeptidase N (APN/CD13), as a zinc-containing ectoenzyme, plays a critical role in the process of tumor angiogenesis, invasion and metastasis. Through the docking-based virtual screening of chemical databases and the further activity assay, we discovered that compound 10c exhibits potent and selective inhibitory ability towards APN. In addition, a series of indoline-2,3-dione derivates have been designed and synthesized as APN inhibitors. The results of preliminary activity evaluation showed that compound 12a (IC50 = 0.074 +/- 0.0026 mu M) exhibited the best inhibitory activity against APN, which could be used for further anticancer agent research. (C) 2012 Published by Elsevier Ltd.

  DOI：

  10.1016/j.bmc.2012.06.024
• 作为产物：
  描述：

  N-(4-bromophenyl)-2-(hydroxyimino) acetamide 在 硫酸 、 对甲苯磺酸 作用下， 以 甲苯 为溶剂， 生成 5'-bromospiro[1,3-dioxepane-2,3'-1H-indole]-2'-one
  参考文献：
  名称：

  Design, synthesis and preliminary biological evaluation of indoline-2,3-dione derivatives as novel HDAC inhibitors

  摘要：

  Histone deacetylases (HDACs) are zinc-dependent or NAD+ dependent enzymes and play a critical role in the process of tumor development. Herein a series of indoline-2,3-dione derivatives have been designed and synthesized as potential HDACs inhibitors. The preliminary biological evaluation showed that most compounds synthesized have exhibited moderate Hela cell nuclear extract inhibitory activities, among which compound 25a (IC50 = 10.13 nM) has shown the best efficacy. The anti-proliferative activities of some of these compounds were also discussed. (C) 2015 Published by Elsevier Ltd.

  DOI：

  10.1016/j.bmc.2015.05.048

文献信息

• Design, synthesis and preliminary biological evaluation of indoline-2,3-dione derivatives as novel HDAC inhibitors
  作者：Kang Jin、Shanshan Li、Xiaoguang Li、Jian Zhang、Wenfang Xu、Xuechen Li

  DOI：10.1016/j.bmc.2015.05.048

  日期：2015.8

  Histone deacetylases (HDACs) are zinc-dependent or NAD+ dependent enzymes and play a critical role in the process of tumor development. Herein a series of indoline-2,3-dione derivatives have been designed and synthesized as potential HDACs inhibitors. The preliminary biological evaluation showed that most compounds synthesized have exhibited moderate Hela cell nuclear extract inhibitory activities, among which compound 25a (IC50 = 10.13 nM) has shown the best efficacy. The anti-proliferative activities of some of these compounds were also discussed. (C) 2015 Published by Elsevier Ltd.
• Novel indoline-2,3-dione derivatives as inhibitors of aminopeptidase N (APN)
  作者：Kang Jin、Xiaopan Zhang、Chunhua Ma、Yingying Xu、Yumei Yuan、Wenfang Xu

  DOI：10.1016/j.bmc.2012.06.024

  日期：2013.5

  Aminopeptidase N (APN/CD13), as a zinc-containing ectoenzyme, plays a critical role in the process of tumor angiogenesis, invasion and metastasis. Through the docking-based virtual screening of chemical databases and the further activity assay, we discovered that compound 10c exhibits potent and selective inhibitory ability towards APN. In addition, a series of indoline-2,3-dione derivates have been designed and synthesized as APN inhibitors. The results of preliminary activity evaluation showed that compound 12a (IC50 = 0.074 +/- 0.0026 mu M) exhibited the best inhibitory activity against APN, which could be used for further anticancer agent research. (C) 2012 Published by Elsevier Ltd.