2-{[4-(2-hydroxyethyl)phenylamino]methyl}-4-methylphenol | 824402-02-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-{[4-(2-hydroxyethyl)phenylamino]methyl}-4-methylphenol
• 英文别名: 2'-hydroxy-5'-methylbenzylamino-4-phenethyl alcohol；2-[[4-(2-Hydroxyethyl)anilino]methyl]-4-methylphenol
• CAS: 824402-02-0
• 化学式: C₁₆H₁₉NO₂
• 分子量: 257.332
• InChiKey: OVFKWNLKDZPGMF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  19
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  52.5
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  聚合甲醛 、 2-{[4-(2-hydroxyethyl)phenylamino]methyl}-4-methylphenol 以 phosphate buffer 、 乙腈 为溶剂， 反应 3.0h， 生成 N-(4'-hydroxyethyl)phenyl-6-methyl-benz[1,3]oxazine
  参考文献：
  名称：

  通过同位素标记和核磁共振光谱表征蛋白质上的三组分偶联反应

  摘要：

  先前开发了一种三组分曼尼希型亲电芳香取代反应，以靶向蛋白质上酪氨酸残基的酚侧链。该反应在温和的条件下进行，为赖氨酸靶向策略提供了方便的替代方案。然而，使用反应性醛，如甲醛，需要仔细检查反应产物，以确保没有发生其他变化。通过使用同位素富集试剂，基于核磁共振 (NMR) 的研究用于获得酪氨酸修饰产物的结构确认。这些实验还揭示了由色氨酸残基的吲哚环产生的反应副产物的形成。半胱氨酸残基显示不参与反应，除了在还原的二硫化物的情况下，形成二硫代缩醛。我们预计这种分析方法将证明对许多生物偶联反应的详细研究有用。

  DOI：

  10.1021/ja710927q
• 作为产物：
  描述：

  N-(4'-hydroxyethyl)phenyl-6-methyl-benz[1,3]oxazine 在 盐酸羟胺 作用下， 以 乙醇 为溶剂， 以0.021 g的产率得到2-{[4-(2-hydroxyethyl)phenylamino]methyl}-4-methylphenol
  参考文献：
  名称：

  A Three-Component Mannich-Type Reaction for Selective Tyrosine Bioconjugation

  摘要：

  A new selective bioconjugation reaction is described for the modification of tyrosine residues on protein substrates. The reaction uses imines formed in situ from aldehydes and electron-rich anilines to modify phenolic side chains through a Mannich-type electrophilic aromatic substitution pathway. The reaction takes place under mild pH and temperature conditions and can modify protein substrates at concentrations as low as 20 muM. Using an efficient fluorescence-based assay, we demonstrated the reaction using a number of aldehydes and protein targets. Importantly, proteins lacking surface-accessible tyrosines remained unmodified. It was also demonstrated that enzymatic activity is preserved under the mild reaction conditions. This strategy represents one of the first carbon-carbon bond-forming reactions for protein modification and provides an important complement to more commonly used lysine- and cysteine-based methods.

  DOI：

  10.1021/ja0439017

文献信息

• Characterization of a Three-Component Coupling Reaction on Proteins by Isotopic Labeling and Nuclear Magnetic Resonance Spectroscopy
  作者：Jesse M. McFarland、Neel S. Joshi、Matthew B. Francis

  DOI：10.1021/ja710927q

  日期：2008.6.18

  tyrosine residues on proteins. This reaction proceeds under mild conditions and provides a convenient alternative to lysine-targeting strategies. However, the use of reactive aldehydes, such as formaldehyde, warrants careful inspection of the reaction products to ensure that other modifications have not occurred. Through the use of isotopically enriched reagents, nuclear magnetic resonance (NMR)-based studies

  先前开发了一种三组分曼尼希型亲电芳香取代反应，以靶向蛋白质上酪氨酸残基的酚侧链。该反应在温和的条件下进行，为赖氨酸靶向策略提供了方便的替代方案。然而，使用反应性醛，如甲醛，需要仔细检查反应产物，以确保没有发生其他变化。通过使用同位素富集试剂，基于核磁共振 (NMR) 的研究用于获得酪氨酸修饰产物的结构确认。这些实验还揭示了由色氨酸残基的吲哚环产生的反应副产物的形成。半胱氨酸残基显示不参与反应，除了在还原的二硫化物的情况下，形成二硫代缩醛。我们预计这种分析方法将证明对许多生物偶联反应的详细研究有用。
• A Three-Component Mannich-Type Reaction for Selective Tyrosine Bioconjugation
  作者：Neel S. Joshi、Leanna R. Whitaker、Matthew B. Francis

  DOI：10.1021/ja0439017

  日期：2004.12.1

  A new selective bioconjugation reaction is described for the modification of tyrosine residues on protein substrates. The reaction uses imines formed in situ from aldehydes and electron-rich anilines to modify phenolic side chains through a Mannich-type electrophilic aromatic substitution pathway. The reaction takes place under mild pH and temperature conditions and can modify protein substrates at concentrations as low as 20 muM. Using an efficient fluorescence-based assay, we demonstrated the reaction using a number of aldehydes and protein targets. Importantly, proteins lacking surface-accessible tyrosines remained unmodified. It was also demonstrated that enzymatic activity is preserved under the mild reaction conditions. This strategy represents one of the first carbon-carbon bond-forming reactions for protein modification and provides an important complement to more commonly used lysine- and cysteine-based methods.