(S)-2-((R)-2-Hydroxy-1-phenyl-ethylamino)-3-(1-nitro-naphthalen-2-yl)-propionitrile | 874620-07-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: (S)-2-((R)-2-Hydroxy-1-phenyl-ethylamino)-3-(1-nitro-naphthalen-2-yl)-propionitrile
• CAS: 874620-07-2
• 化学式: C₂₁H₁₉N₃O₃
• 分子量: 361.4
• InChiKey: QFBHJMMBFLOPTE-ICSRJNTNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.51
• 重原子数：
  27.0
• 可旋转键数：
  7.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  99.19
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  (S)-2-((R)-2-Hydroxy-1-phenyl-ethylamino)-3-(1-nitro-naphthalen-2-yl)-propionitrile 在 palladium on activated charcoal 盐酸 、 锂硼氢 、 氢气 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 20.0 ℃ 、101.33 kPa 条件下， 反应 34.5h， 生成 (S)-3-(1-Amino-naphthalen-2-yl)-2-((R)-2-hydroxy-1-phenyl-ethylamino)-propan-1-ol
  参考文献：
  名称：

  Indolactam-V Is Involved in the CH/π Interaction with Pro-11 of the PKCδ C1B Domain:  Application for the Structural Optimization of the PKCδ Ligand

  摘要：

  The CH/pi interaction between the indole ring of indolactam-V (IL-V) and the hydrogen atom at position 4 of Pro-11 of the PKCdelta C1B domain was evaluated using the mutant peptide of the PKCdelta C1B domain, in which the CH/pi interaction was inhibited by substitution of the hydrogen atom with a fluorine atom. IL-V showed about a 10 times lower binding affinity to the mutant peptide compared to the wild-type peptide, suggesting that the CH/pi interaction could play a pivotal role in the binding of IL-V to the PKCdelta C1B domain. On the other hand, benzolactam-V8 (BL-V8), with the benzene ring instead of the indole ring of IL-V, might lack the CH/pi interaction. The low binding affinity of BL-V8 could be enhanced by the effective formation of the CH/pi interaction as exemplified by the synthesis of naphtholactam-V8 (NL-V8).

  DOI：

  10.1021/ja050447d
• 作为产物：
  描述：

  2-(2,2-Dimethoxyethyl)-1-nitronaphthalene 在 三氟乙酸 作用下， 以 甲醇 、 氯仿 为溶剂， 反应 8.0h， 生成 (S)-2-((R)-2-Hydroxy-1-phenyl-ethylamino)-3-(1-nitro-naphthalen-2-yl)-propionitrile
  参考文献：
  名称：

  Indolactam-V Is Involved in the CH/π Interaction with Pro-11 of the PKCδ C1B Domain:  Application for the Structural Optimization of the PKCδ Ligand

  摘要：

  The CH/pi interaction between the indole ring of indolactam-V (IL-V) and the hydrogen atom at position 4 of Pro-11 of the PKCdelta C1B domain was evaluated using the mutant peptide of the PKCdelta C1B domain, in which the CH/pi interaction was inhibited by substitution of the hydrogen atom with a fluorine atom. IL-V showed about a 10 times lower binding affinity to the mutant peptide compared to the wild-type peptide, suggesting that the CH/pi interaction could play a pivotal role in the binding of IL-V to the PKCdelta C1B domain. On the other hand, benzolactam-V8 (BL-V8), with the benzene ring instead of the indole ring of IL-V, might lack the CH/pi interaction. The low binding affinity of BL-V8 could be enhanced by the effective formation of the CH/pi interaction as exemplified by the synthesis of naphtholactam-V8 (NL-V8).

  DOI：

  10.1021/ja050447d