H-ILKEPVHGY-SCH₂CH₂CO₂H | 1271876-09-5

• 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: H-ILKEPVHGY-SCH₂CH₂CO₂H
• 英文别名: (4S)-4-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-amino-3-methylpentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]amino]-5-[(2S)-2-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-(2-carboxyethylsulfanyl)-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-3-(1H-imidazol-5-yl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]carbamoyl]pyrrolidin-1-yl]-5-oxopentanoic acid
• CAS: 1271876-09-5
• 化学式: C₅₃H₈₂N₁₂O₁₄S
• 分子量: 1143.37
• InChiKey: WUXLBAWLWJIYAA-FQVFVWHVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.2
• 重原子数：
  80
• 可旋转键数：
  36
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  442
• 氢给体数：
  13
• 氢受体数：
  18

反应信息

• 作为产物：
  描述：

  在 氧气 、 三(2-羰基乙基)磷盐酸盐 、 碳酸氢铵 、 sodium hydroxide 作用下， 以 水 为溶剂， 反应 16.0h， 生成 H-ILKEPVHGY-SCH₂CH₂CO₂H
  参考文献：
  名称：

  Synthesis of Peptide Alkylthioesters Using the Intramolecular N,S-Acyl Shift Properties of Bis(2-sulfanylethyl)amido Peptides

  摘要：

  The design of novel methods giving access to peptide alkylthioesters, the key building blocks for protein synthesis using Native Chemical Ligation, is an important area of research. Bis(2-sulfanylethyl)amido peptides (SEA peptides) 1 equilibrate in aqueous solution with S-2-(2-mercaptoethylamino)ethyl thioester peptides 2 through an N,S-acyl shift mechanism. HPLC was used to study the rate of equilibration for different C-terminal amino acids and the position of equilibrium as a function of pH. We show also that thioester form 2 can participate efficiently in a thiol-thioester exchange reaction with 5% aqueous 3-mercaptopropionic acid. The highest reaction rate was obtained at pH 4. These experimental conditions are significantly less acidic than those reported in the past for related systems. The method was validated with the synthesis of a 24-mer peptide thioester. Consequently, SEA peptides 1 constitute a powerful platform for access to native chemical ligation methodologies.

  DOI：

  10.1021/jo200029e

文献信息

• Insight into the SEA amide thioester equilibrium. Application to the synthesis of thioesters at neutral pH
  作者：S. L. Pira、O. El Mahdi、L. Raibaut、H. Drobecq、J. Dheur、E. Boll、O. Melnyk

  DOI：10.1039/c6ob01079b

  日期：——

  bis(2-sulfanylethyl)amide (SEA) N,S-acyl shift thioester surrogate has found a variety of useful applications in the field of protein total synthesis. Here we present novel insights into the SEA amide/thioester equilibrium in water which is an essential step in any reaction involving the thioester surrogate properties of the SEA group. We also show that the SEA amide thioester equilibrium can be efficiently displaced

  的双（2-硫烷基乙基）酰胺（SEA）Ñ，小号酰基蛋白质总合成领域的各种有用的应用转移硫酯替代发现了。在这里，我们介绍了水中SEA酰胺/硫酯平衡的新颖见解，这是任何涉及SEA组硫酯替代性质的反应中必不可少的步骤。我们还表明，SEA酰胺硫代酸酯平衡可以在中性pH下有效地置换，以获取肽烷基硫代酸酯，即天然化学连接（NCL）反应的关键组分。
• Synthesis of Peptide Alkylthioesters Using the Intramolecular <i>N</i>,<i>S</i>-Acyl Shift Properties of Bis(2-sulfanylethyl)amido Peptides
  作者：Julien Dheur、Nathalie Ollivier、Aurélie Vallin、Oleg Melnyk

  DOI：10.1021/jo200029e

  日期：2011.5.6

  The design of novel methods giving access to peptide alkylthioesters, the key building blocks for protein synthesis using Native Chemical Ligation, is an important area of research. Bis(2-sulfanylethyl)amido peptides (SEA peptides) 1 equilibrate in aqueous solution with S-2-(2-mercaptoethylamino)ethyl thioester peptides 2 through an N,S-acyl shift mechanism. HPLC was used to study the rate of equilibration for different C-terminal amino acids and the position of equilibrium as a function of pH. We show also that thioester form 2 can participate efficiently in a thiol-thioester exchange reaction with 5% aqueous 3-mercaptopropionic acid. The highest reaction rate was obtained at pH 4. These experimental conditions are significantly less acidic than those reported in the past for related systems. The method was validated with the synthesis of a 24-mer peptide thioester. Consequently, SEA peptides 1 constitute a powerful platform for access to native chemical ligation methodologies.