4-(2'-carbomethoxy-1'-pyrrolidinyl)-5-methyl-1,2-benzoquinone

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 4-(2'-carbomethoxy-1'-pyrrolidinyl)-5-methyl-1,2-benzoquinone
• 英文别名: methyl (2S)-1-(6-methyl-3,4-dioxocyclohexa-1,5-dien-1-yl)pyrrolidine-2-carboxylate
• 化学式: C₁₃H₁₅NO₄
• 分子量: 249.266
• InChiKey: SKVAJYDINGJDCO-VIFPVBQESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.61
• 重原子数：
  18.0
• 可旋转键数：
  2.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  63.68
• 氢给体数：
  0.0
• 氢受体数：
  5.0

反应信息

• 作为产物：
  描述：

  L-脯氨酸甲酯盐酸盐 、 邻氨基对甲苯酚 在 potassium hexacyanoferrate(III) 作用下， 以 aq. phosphate buffer 、 乙腈 为溶剂， 生成 4-(2'-carbomethoxy-1'-pyrrolidinyl)-5-methyl-1,2-benzoquinone
  参考文献：
  名称：

  N-Terminal Modification of Proteins with o-Aminophenols

  摘要：

  The synthetic modification of proteins plays an important role in chemical biology and biomaterials science. These fields provide a constant need for chemical tools that can introduce new functionality in specific locations on protein surfaces. In this work, an oxidative strategy is demonstrated for the efficient modification of N-terminal residues on peptides and N-terminal proline residues on proteins. The strategy uses o-aminophenols or o-catechols that are oxidized to active coupling species in situ using potassium ferricyanide. Peptide screening results have revealed that many N-terminal amino acids can participate in this reaction, and that proline residues are particularly reactive. When applied to protein substrates, the reaction shows a stronger requirement for the proline group. Key advantages of the reaction include its fast second-order kinetics and ability to achieve site-selective modification in a single step using low concentrations of reagent. Although free cysteines are also modified by the coupling reaction, they can be protected through disulfide formation and then liberated after N-terminal coupling is complete. This allows access to doubly functionalized bioconjugates that can be difficult to access using other methods.

  DOI：

  10.1021/ja500728c

文献信息

• Secondary modification of oxidatively-modified proline N-termini for the construction of complex bioconjugates
  作者：Johnathan C. Maza、Alexandra V. Ramsey、Meire Mehare、Shane W. Krska、Craig A. Parish、Matthew B. Francis

  DOI：10.1039/d0ob00211a

  日期：——

  A sequential oxidative coupling and oxime or hydrazone ligation method allows construction of bifunctional N-terminal bioconjugates.

  一种顺序氧化偶联和肟或缩醛缀合方法允许构建具有双功能N-末端生物结合物。
• Formation of Strecker Aldehydes from Polyphenol-Derived Quinones and α-Amino Acids in a Nonenzymic Model System
  作者：George P. Rizzi

  DOI：10.1021/jf052781z

  日期：2006.3.1

  vegetables contain naturally occurring polyphenolic compounds that can undergo enzyme-catalyzed oxidation during food preparation. Many of these compounds contain catechol (1,2-dihydroxybenzene) moieties that may be transformed into o-quinone derivatives by polyphenoloxidases and molecular oxygen. Secondary reactions of the o-quinones include the Strecker degradation of ambient amino acids to form flavor-important

  水果和蔬菜包含天然存在的多酚化合物，在食物制备过程中会经历酶催化的氧化。这些化合物中许多都含有邻苯二酚（1,2-二羟基苯）部分，可通过多酚氧化酶和分子氧将其转化为邻苯二酚衍生物。邻醌的次级反应包括环境氨基酸的Strecker降解，从而形成重要的风味挥发性醛。这项工作的目的是研究非酶模型系统中多酚/邻醌/ Strecker降解序列的机理。通过在22摄氏度的pH值为7.17的磷酸盐缓冲液中使用铁氰化物离子作为氧化剂，咖啡酸，绿原酸，（+）儿茶素，使（-）表儿茶素和（-）表儿茶素与蛋氨酸和苯丙氨酸反应生成摩尔浓度为0.032-0.42％（反应混合物中为0.7-10 ppm）的斯特雷克醛蛋氨酸和苯乙醛。另外，通过在与4-甲基邻苯二酚的反应中使用1-脯氨酸甲酯，得到了关键的反应中间体4-（2'-羰甲氧基-1'-吡咯烷基）-5-甲基-1,2-苯醌（7）。孤立并初步确定。
• N-Terminal Modification of Proteins with <i>o</i>-Aminophenols
  作者：Allie C. Obermeyer、John B. Jarman、Matthew B. Francis

  DOI：10.1021/ja500728c

  日期：2014.7.9

  The synthetic modification of proteins plays an important role in chemical biology and biomaterials science. These fields provide a constant need for chemical tools that can introduce new functionality in specific locations on protein surfaces. In this work, an oxidative strategy is demonstrated for the efficient modification of N-terminal residues on peptides and N-terminal proline residues on proteins. The strategy uses o-aminophenols or o-catechols that are oxidized to active coupling species in situ using potassium ferricyanide. Peptide screening results have revealed that many N-terminal amino acids can participate in this reaction, and that proline residues are particularly reactive. When applied to protein substrates, the reaction shows a stronger requirement for the proline group. Key advantages of the reaction include its fast second-order kinetics and ability to achieve site-selective modification in a single step using low concentrations of reagent. Although free cysteines are also modified by the coupling reaction, they can be protected through disulfide formation and then liberated after N-terminal coupling is complete. This allows access to doubly functionalized bioconjugates that can be difficult to access using other methods.