ILKEPVHGA-SEA^off | 1255709-31-9

• 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: ILKEPVHGA-SEA^off
• 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-(1,2,5-dithiazepan-5-yl)-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: 1255709-31-9
• 化学式: C₄₈H₈₁N₁₃O₁₁S₂
• 分子量: 1080.38
• InChiKey: XMEIYAGNLAYIPK-MHCXGOGJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.1
• 重原子数：
  74
• 可旋转键数：
  30
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.73
• 拓扑面积：
  413
• 氢给体数：
  11
• 氢受体数：
  16

反应信息

• 作为反应物：
  描述：

  ILKEPVHGA-SEA^off 在 三(2-羰基乙基)磷盐酸盐 、 sodium hydroxide 作用下， 反应 0.5h， 生成 ILKEPVHGA-SEA^on
  参考文献：
  名称：

  深入了解SEA酰胺硫酯平衡。在中性pH下用于合成硫酯的应用†

  摘要：

  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。

  DOI：

  10.1039/c6ob01079b
• 作为产物：
  描述：

  ILKEPVHGA-SEA^on 在 碘 、 溶剂黄146 作用下， 以 水 为溶剂， 生成 ILKEPVHGA-SEA^off
  参考文献：
  名称：

  一种让人联想到水生化学的铁催化蛋白质脱硫方法

  摘要：

  在碳酸氢盐缓冲液中的有氧条件下，通过微摩尔浓度的铁可以有效地实现磷化氢对半胱氨酸的脱硫。脱硫机制可能涉及通过分子氧氧化铁（II）-碳酸盐络合物产生的铁（III）物质，让人联想到天然水中发生的铁催化氧化现象。

  DOI：

  10.1002/anie.202302648

文献信息

• Accelerating chemoselective peptide bond formation using bis(2-selenylethyl)amido peptide selenoester surrogates
  作者：Laurent Raibaut、Marine Cargoët、Nathalie Ollivier、Yun Min Chang、Hervé Drobecq、Emmanuelle Boll、Rémi Desmet、Jean-Christophe M. Monbaliu、Oleg Melnyk

  DOI：10.1039/c5sc03459k

  日期：——

  SeEA latent selenoester: go fast by switching to selenium.

  SeEA 潜在硒酯：通过改用硒来加快速度。
• Bis(2-sulfanylethyl)amino Native Peptide Ligation
  作者：Nathalie Ollivier、Julien Dheur、Reda Mhidia、Annick Blanpain、Oleg Melnyk

  DOI：10.1021/ol102273u

  日期：2010.11.19

  The reaction of a peptide featuring a bis(2-sulfanylethyl)amino (SEA) group on its C-terminus with a cysteinyl peptide in water at pH 7 and 37 C leads to the chemoselective and regioselective formation of a native peptide bond. This method called SEA ligation enriches the native peptide ligation repertoire available to the peptide chemist. Preparation of an innovative solid support which allows the straightforward synthesis of peptide SEA fragments using standard Fmoc/fert-butyl solid phase peptide synthesis procedures is also described.
• Synthesis of Peptide Thioacids at Neutral pH Using Bis(2-sulfanylethyl)amido Peptide Precursors
  作者：Silvain L. Pira、Emmanuelle Boll、Oleg Melnyk

  DOI：10.1021/ol402601j

  日期：2013.10.18

  Reaction of bis(2-sulfanylethyl)amido (SEA) peptides with trilsopropylsilylthiol in water at neutral pH yields peptide thiocarboxylates. An alkylthioester derived from beta-alanine was used to trap the released bis(2-sulfanylethyl)amine and displace the equilibrium toward the peptide thiocarboxylate.
• 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.
• Selenopeptide Transamidation and Metathesis
  作者：Nathalie Ollivier、Annick Blanpain、Emmanuelle Boll、Laurent Raibaut、Hervé Drobecq、Oleg Melnyk

  DOI：10.1021/ol501866j

  日期：2014.8.1

  Selenopeptides can be transamidated by cysteinyl peptides in water using mild conditions (pH 5.5, 37 °C) in the presence of an arylthiol catalyst. Similar conditions also catalyze the metathesis of selenopeptides. The usefulness of the selenophosphine derived from TCEP (TCEP═Se) for inhibiting the TCEP-induced deselenization of selenocysteine residue is also reported.