3t-(4-amino-phenyl)-2-methyl-acrylaldehyde | 52338-39-3

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 肉桂醛
• 英文名称: 3t-(4-amino-phenyl)-2-methyl-acrylaldehyde
• 英文别名: 3t-(4-Amino-phenyl)-2-methyl-acrylaldehyd；(E)-3-(4-aminophenyl)-2-methylprop-2-enal
• CAS: 52338-39-3
• 化学式: C₁₀H₁₁NO
• 分子量: 161.203
• InChiKey: GZJPWKIMIFGBHT-SOFGYWHQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  12
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  43.1
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  3t-(4-amino-phenyl)-2-methyl-acrylaldehyde 在 盐酸 、 4 A molecular sieve 、 sodium acetate 、 sodium sulfate 、 尿素 、 sodium nitrite 作用下， 以 甲醇 为溶剂， 生成
  参考文献：
  名称：

  Novel Bacteriorhodopsin Analogues Based on Azo Chromophores

  摘要：

  Bacteriorhodopsin analogues BR-I, BR-II and BR-III containing azo chromophores 4-[[4'-(N,N-dimethylamino)phenyl- 1']azo]benzaldehyde, 3-[4-[[4'-(N,N-dimethylamino)phenyl-1']azo]phenyl-l]prop-2-enal and 3-[4-[[4'-(N,N-dimethylamino)phenyl-1']azo]phenyl-l]-2-methylprop-2-enal, respectively, were prepared and characterized by UV-vis spectroscopy, opsin shift, competitive binding with retinal, fluorescence spectroscopy, light-induced pH change, and flash photolysis. BR-I, BR-II, and BR-III had UV-vis absorption maxima at 458, 597, and 485 nm and opsin shifts of -329, 3091, and 43 cm(-1), respectively. Competitive binding studies showed that the azo chromophores could not be easily displaced by retinal. Quenching of protein fluorescence by the azo chromophores indicated intimate interactions occurring between the respective azo chromophores and the protein bound residues. The proteins were also found to show functional characteristics (light-induced pH change and flash photolysis profiles) different from those of native bacteriorhodopsin. The results are discussed in terms of the nature of interaction between the azo chromophore and the surrounding protein.

  DOI：

  10.1021/ja954286x
• 作为产物：
  描述：

  (E)-2-methyl-3-(4-nitrophenyl)acrylaldehyde 在 氨 、 iron(II) sulfate 作用下， 生成 3t-(4-amino-phenyl)-2-methyl-acrylaldehyde
  参考文献：
  名称：

  Naito et al., Nippon Kagaku Zasshi, 1958, vol. 79, p. 374,378

  摘要：

  DOI：

文献信息

• Naito et al., Nippon Kagaku Zasshi, 1958, vol. 79, p. 374,378
  作者：Naito et al.

  DOI：——

  日期：——
• US7576079B2
  申请人：——

  公开号：US7576079B2

  公开（公告）日：2009-08-18
• Novel Bacteriorhodopsin Analogues Based on Azo Chromophores
  作者：Anil K. Singh、Joydip Das、Nirmalya Majumdar

  DOI：10.1021/ja954286x

  日期：1996.1.1

  Bacteriorhodopsin analogues BR-I, BR-II and BR-III containing azo chromophores 4-[[4'-(N,N-dimethylamino)phenyl- 1']azo]benzaldehyde, 3-[4-[[4'-(N,N-dimethylamino)phenyl-1']azo]phenyl-l]prop-2-enal and 3-[4-[[4'-(N,N-dimethylamino)phenyl-1']azo]phenyl-l]-2-methylprop-2-enal, respectively, were prepared and characterized by UV-vis spectroscopy, opsin shift, competitive binding with retinal, fluorescence spectroscopy, light-induced pH change, and flash photolysis. BR-I, BR-II, and BR-III had UV-vis absorption maxima at 458, 597, and 485 nm and opsin shifts of -329, 3091, and 43 cm(-1), respectively. Competitive binding studies showed that the azo chromophores could not be easily displaced by retinal. Quenching of protein fluorescence by the azo chromophores indicated intimate interactions occurring between the respective azo chromophores and the protein bound residues. The proteins were also found to show functional characteristics (light-induced pH change and flash photolysis profiles) different from those of native bacteriorhodopsin. The results are discussed in terms of the nature of interaction between the azo chromophore and the surrounding protein.