(1-nitro-[2]naphthyl)-acetaldehyde | 861354-92-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: (1-nitro-[2]naphthyl)-acetaldehyde
• 英文别名: β-Oxo-α-(1-nitro-naphthyl-(2))-aethan；(1-Nitro-[2]naphthyl)-acetaldehyd；2-(1-Nitronaphthalen-2-yl)acetaldehyde
• CAS: 861354-92-9
• 化学式: C₁₂H₉NO₃
• 分子量: 215.208
• InChiKey: IVCVDKUOIAOSLU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  16
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  62.9
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (1-nitro-[2]naphthyl)-acetaldehyde 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， 40.0 ℃ 、101.33 kPa 条件下， 反应 100.5h， 生成
  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-甲基-二硝基萘酚 在 camphor-10-sulfonic acid 、 三氟乙酸 作用下， 以 氯仿 、 N,N-二甲基甲酰胺 为溶剂， 反应 29.0h， 生成 (1-nitro-[2]naphthyl)-acetaldehyde
  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

文献信息

• Mayer,F.; Oppenheimer, Chemische Berichte, 1918, vol. 51, p. 1243
  作者：Mayer,F.、Oppenheimer

  DOI：——

  日期：——