rhodamine B 4-(3-(succinimidooxycarbonyloxy)propyl)piperazine amide | 608136-14-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• 英文名称: rhodamine B 4-(3-(succinimidooxycarbonyloxy)propyl)piperazine amide
• 英文别名: [6-(Diethylamino)-9-[2-[4-[3-(2,5-dioxopyrrolidin-1-yl)oxycarbonyloxypropyl]piperazine-1-carbonyl]phenyl]xanthen-3-ylidene]-diethylazanium；[6-(diethylamino)-9-[2-[4-[3-(2,5-dioxopyrrolidin-1-yl)oxycarbonyloxypropyl]piperazine-1-carbonyl]phenyl]xanthen-3-ylidene]-diethylazanium
• CAS: 608136-14-7
• 化学式: C₄₀H₄₈N₅O₇
• 分子量: 710.85
• InChiKey: ISHZPGYHRZHXRC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  52
• 可旋转键数：
  14
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  112
• 氢给体数：
  0
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  2-(4-氨基苯)乙胺 、 rhodamine B 4-(3-(succinimidooxycarbonyloxy)propyl)piperazine amide 在 吡啶 作用下， 反应 2.0h， 生成 rhodamine B 4-(3-[2-(4-aminophenyl)ethyl]carbamoyloxypropyl)piperazine amide
  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
• 作为产物：
  描述：

  溶剂红 49 在 吡啶 、 三甲基铝 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 、 甲苯 为溶剂， 反应 58.0h， 生成 rhodamine B 4-(3-(succinimidooxycarbonyloxy)propyl)piperazine amide
  参考文献：
  名称：

  实用的合成路线到罗丹明染料。

  摘要：

  [反应：见正文]已经开发了一种合成功能化若丹明衍生物的有效方法。可以从廉价的前体制备数克量的这些水溶性荧光团，并在不使用色谱法的情况下进行纯化。通过后续反应已安装了一系列蛋白质反应性官能团，为生物分子修饰提供了材料。对于多色应用，已开发出一种固相纯化策略，以提供具有广泛光谱特性的罗丹明衍生物。

  DOI：

  10.1021/ol035135z

文献信息

• Practical Synthetic Route to Functionalized Rhodamine Dyes
  作者：Trung Nguyen、Matthew B. Francis

  DOI：10.1021/ol035135z

  日期：2003.9.1

  [reaction: see text] An efficient method for the synthesis of functionalized rhodamine derivatives has been developed. Multigram quantities of these water-soluble fluorophores can be prepared from inexpensive precursors and purified without the use of chromatography. A series of protein-reactive functional groups has been installed through subsequent reactions, providing materials for biomolecule modification

  [反应：见正文]已经开发了一种合成功能化若丹明衍生物的有效方法。可以从廉价的前体制备数克量的这些水溶性荧光团，并在不使用色谱法的情况下进行纯化。通过后续反应已安装了一系列蛋白质反应性官能团，为生物分子修饰提供了材料。对于多色应用，已开发出一种固相纯化策略，以提供具有广泛光谱特性的罗丹明衍生物。
• 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.