benzyl (2S)-2-[[1-hexyl-3-[(3S)-4-hydroxy-3-[(2-methylpropan-2-yl)oxycarbonylamino]butyl]indol-4-yl]-methylamino]-3-methylbutanoate | 1004551-06-7

• 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: benzyl (2S)-2-[[1-hexyl-3-[(3S)-4-hydroxy-3-[(2-methylpropan-2-yl)oxycarbonylamino]butyl]indol-4-yl]-methylamino]-3-methylbutanoate
• CAS: 1004551-06-7
• 化学式: C₃₆H₅₃N₃O₅
• 分子量: 607.834
• InChiKey: NSFSWVIRMNSPHJ-ZQAZVOLISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.9
• 重原子数：
  44
• 可旋转键数：
  19
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  93
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  benzyl (2S)-2-[[1-hexyl-3-[(3S)-4-hydroxy-3-[(2-methylpropan-2-yl)oxycarbonylamino]butyl]indol-4-yl]-methylamino]-3-methylbutanoate 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 为溶剂， 20.0 ℃ 、101.33 kPa 条件下， 反应 1.0h， 生成
  参考文献：
  名称：

  Synthesis, Conformational Analysis, and Biological Evaluation of 1-Hexylindolactam-V10 as a Selective Activator for Novel Protein Kinase C Isozymes

  摘要：

  Conventional and novel protein kinase C (PKC) isozymes are the main targets of tumor promoters. We developed 1-hexylindolactam-V10 (5) as a selective activator for novel PKC isozymes that play important roles in various cellular processes related to tumor promotion, ischemia-reperfusion injury in the heart, and Alzheimer's disease. The compound existed as a mixture of three conformers. The trans-amide restricted analogues of 5 (14 and 15) hardly bound to PKC isozymes, suggesting that the active conformation of 5 could be that with a cis-amide. Compound 5 selectively translocated novel PKC isozymes over conventional PKC isozymes in HeLa cells at 0.1-1 mu M. These results suggest that 5 could be useful for the functional analysis of novel PKC isozymes.

  DOI：

  10.1021/jm0706719
• 作为产物：
  描述：

  tert-butyl N-[(2S)-4-[1-hexyl-4-(methylamino)indol-3-yl]-1-hydroxybutan-2-yl]carbamate 、 benzyl (R)-4-methyl-2-(trifluoromethylsulfonyloxy)pentanoate 在 2,6-二甲基吡啶 作用下， 以 1,2-二氯乙烷 为溶剂， 反应 22.0h， 以44%的产率得到benzyl (2S)-2-[[1-hexyl-3-[(3S)-4-hydroxy-3-[(2-methylpropan-2-yl)oxycarbonylamino]butyl]indol-4-yl]-methylamino]-3-methylbutanoate
  参考文献：
  名称：

  Synthesis, Conformational Analysis, and Biological Evaluation of 1-Hexylindolactam-V10 as a Selective Activator for Novel Protein Kinase C Isozymes

  摘要：

  Conventional and novel protein kinase C (PKC) isozymes are the main targets of tumor promoters. We developed 1-hexylindolactam-V10 (5) as a selective activator for novel PKC isozymes that play important roles in various cellular processes related to tumor promotion, ischemia-reperfusion injury in the heart, and Alzheimer's disease. The compound existed as a mixture of three conformers. The trans-amide restricted analogues of 5 (14 and 15) hardly bound to PKC isozymes, suggesting that the active conformation of 5 could be that with a cis-amide. Compound 5 selectively translocated novel PKC isozymes over conventional PKC isozymes in HeLa cells at 0.1-1 mu M. These results suggest that 5 could be useful for the functional analysis of novel PKC isozymes.

  DOI：

  10.1021/jm0706719

文献信息

• Synthesis, Conformational Analysis, and Biological Evaluation of 1-Hexylindolactam-V10 as a Selective Activator for Novel Protein Kinase C Isozymes
  作者：Ryo C. Yanagita、Yu Nakagawa、Nobuhiro Yamanaka、Kaori Kashiwagi、Naoaki Saito、Kazuhiro Irie

  DOI：10.1021/jm0706719

  日期：2008.1.1

  Conventional and novel protein kinase C (PKC) isozymes are the main targets of tumor promoters. We developed 1-hexylindolactam-V10 (5) as a selective activator for novel PKC isozymes that play important roles in various cellular processes related to tumor promotion, ischemia-reperfusion injury in the heart, and Alzheimer's disease. The compound existed as a mixture of three conformers. The trans-amide restricted analogues of 5 (14 and 15) hardly bound to PKC isozymes, suggesting that the active conformation of 5 could be that with a cis-amide. Compound 5 selectively translocated novel PKC isozymes over conventional PKC isozymes in HeLa cells at 0.1-1 mu M. These results suggest that 5 could be useful for the functional analysis of novel PKC isozymes.