tert-butyl (6-(cyclohexylamino)hexyl)carbamate | 239064-32-5

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: tert-butyl (6-(cyclohexylamino)hexyl)carbamate
• 英文别名: tert-butyl N-[6-(cyclohexylamino)hexyl]carbamate
• CAS: 239064-32-5
• 化学式: C₁₇H₃₄N₂O₂
• 分子量: 298.469
• InChiKey: DPQNIMVMCIYKNE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  21
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.94
• 拓扑面积：
  50.4
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  tert-butyl (6-(cyclohexylamino)hexyl)carbamate 在 哌啶 、 N-甲基吗啉 、 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 22.25h， 生成 tert-butyl N-[6-[cyclohexyl-[(2S)-2-[[(2R,3R)-3-methyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoyl]amino]-3-phenylpropanoyl]amino]hexyl]carbamate
  参考文献：
  名称：

  4-Heterocyclohexanone-Based Inhibitors of the Serine Protease Plasmin

  摘要：

  Three inhibitors that are based upon a 4-heterocyclohexanone nucleus were synthesized and evaluated for activity against the serine protease plasmin. Inhibitors of plasmin have potential as cancer chemotherapeutic agents that act by blocking both angiogenesis and metastasis. Inhibitor 1 has moderate activity against plasmin but shows good selectivity for this enzyme compared to other serine proteases including trypsin, thrombin, and kallikrein. Inhibitor 2 shows both good activity and selectivity for plasmin. Inhibitor 3, which does not incorporate an aminohexyl group that can interact with the S1 subsite, has poor activity. These results, along with previous work, demonstrate that the 4-heterocyclohexanone nucleus can effectively serve as the basis for designing inhibitors of both serine and cyst;eine proteases.

  DOI：

  10.1021/jm990110k
• 作为产物：
  描述：

  N-(6-羟基己基)氨基甲酸叔丁酯 在 aluminum oxide 、 三乙酰氧基硼氢化钠 、 pyridinium chlorochromate 作用下， 以 二氯甲烷 、 1,2-二氯乙烷 为溶剂， 反应 6.0h， 生成 tert-butyl (6-(cyclohexylamino)hexyl)carbamate
  参考文献：
  名称：

  4-Heterocyclohexanone-Based Inhibitors of the Serine Protease Plasmin

  摘要：

  Three inhibitors that are based upon a 4-heterocyclohexanone nucleus were synthesized and evaluated for activity against the serine protease plasmin. Inhibitors of plasmin have potential as cancer chemotherapeutic agents that act by blocking both angiogenesis and metastasis. Inhibitor 1 has moderate activity against plasmin but shows good selectivity for this enzyme compared to other serine proteases including trypsin, thrombin, and kallikrein. Inhibitor 2 shows both good activity and selectivity for plasmin. Inhibitor 3, which does not incorporate an aminohexyl group that can interact with the S1 subsite, has poor activity. These results, along with previous work, demonstrate that the 4-heterocyclohexanone nucleus can effectively serve as the basis for designing inhibitors of both serine and cyst;eine proteases.

  DOI：

  10.1021/jm990110k

文献信息

• Highly Selective Reductive Cross-Amination between Aniline or Nitroarene Derivatives and Alkylamines Catalyzed by Polysilane-Immobilized Rh/Pt Bimetallic Nanoparticles
  作者：Aya Suzuki、Hiroyuki Miyamura、Shū Kobayashi

  DOI：10.1055/s-0037-1611341

  日期：2019.3

  partial hydrogenation of aniline or nitroarene derivatives and alkylamines is an ideal method for obtaining N-alkylated cyclohexylamine derivatives; however, no such transformations have hitherto been established. Here, we report a highly selective reductive cross-amination using aniline derivatives and alkylamines catalyzed by heterogeneous Rh/Pt bimetallic nanoparticles under mild conditions. The catalyst

  苯胺或硝基芳烃衍生物部分加氢生成的亚胺中间体与烷基胺之间的还原性交叉胺化是获得N-烷基化环己胺衍生物的理想方法；然而，迄今为止还没有建立这样的转变。在这里，我们报告了使用苯胺衍生物和烷基胺在温和条件下由非均相 Rh/Pt 双金属纳米粒子催化的高选择性还原交叉胺化。催化剂被回收并重复使用五次，保持高活性。在该反应中，苯胺衍生物部分加氢过程中产生的亚胺中间体被伯烷基胺与催化剂的强烈相互作用立即捕获，导致高度选择性的转化，得到所需的产物，
• 4-Heterocyclohexanone-Based Inhibitors of the Serine Protease Plasmin
  作者：Tanya C. Sanders、Christopher T. Seto

  DOI：10.1021/jm990110k

  日期：1999.7.1

  Three inhibitors that are based upon a 4-heterocyclohexanone nucleus were synthesized and evaluated for activity against the serine protease plasmin. Inhibitors of plasmin have potential as cancer chemotherapeutic agents that act by blocking both angiogenesis and metastasis. Inhibitor 1 has moderate activity against plasmin but shows good selectivity for this enzyme compared to other serine proteases including trypsin, thrombin, and kallikrein. Inhibitor 2 shows both good activity and selectivity for plasmin. Inhibitor 3, which does not incorporate an aminohexyl group that can interact with the S1 subsite, has poor activity. These results, along with previous work, demonstrate that the 4-heterocyclohexanone nucleus can effectively serve as the basis for designing inhibitors of both serine and cyst;eine proteases.