3-(2-amino-ethyldisulfanyl)-L-alanine | 22801-37-2

• 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: 3-(2-amino-ethyldisulfanyl)-L-alanine
• 英文别名: (R)-2-Amino-3-(2-amino-aethyldisulfanyl)-propionsaeure；3-(2-Amino-aethyldisulfanyl)-L-alanin；L-Cystein-cysteamindisulfid；3-[(2-Aminoethyl)disulfanyl]-L-alanine；(2R)-2-amino-3-(2-aminoethyldisulfanyl)propanoic acid
• CAS: 22801-37-2
• 化学式: C₅H₁₂N₂O₂S₂
• 分子量: 196.294
• InChiKey: WYQFVGPQTGCDJH-BYPYZUCNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.6
• 重原子数：
  11
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  140
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  S-(ethylsulfonyl)-L-cysteine 、 巯基乙胺 以 重水 为溶剂， 生成 3-(2-amino-ethyldisulfanyl)-L-alanine
  参考文献：
  名称：

  硫醇和二硫化物：在合成肽和聚合物中化学选择性形成不对称二硫化物的方法

  摘要：

  在蛋白质或肽化学中，硫醇经常被选作化学选择性修饰反应的化学实体。尽管这是解决在水性介质中形成半胱氨酸键的半胱氨酸和高半胱氨酸的成熟方法，但是，化学选择性形成不对称二硫键的可能性却很少。关注共轭化学中的生物可逆性，对于将含硫醇的生物活性剂连接到蛋白质或进行交联反应而言，形成二硫键是非常可取的，因为二硫键可以将血液中的稳定性与细胞内的可降解性结合在一起。在此概念文章中，重点介绍了肽和聚合物材料中掺入的巯基部分的活化基团领域中的最新方法。探索了在材料合成过程中对硫醇具有高反应性的稳定性的有利组合，其重点在于简化和防止副反应以及在二硫化物形成之前进行的其他脱保护和活化步骤。此外，突出了这种化学的应用，并展望了未来的前景。

  DOI：

  10.1002/chem.201800681

文献信息

• Rethinking Cysteine Protective Groups:<i>S</i>-Alkylsulfonyl-<scp>l</scp>-Cysteines for Chemoselective Disulfide Formation
  作者：Olga Schäfer、David Huesmann、Christian Muhl、Matthias Barz

  DOI：10.1002/chem.201604391

  日期：2016.12.12

  The ability to reversibly cross‐link proteins and peptides grants the amino acid cysteine its unique role in nature as well as in peptide chemistry. We report a novel class of S‐alkylsulfonyl‐l‐cysteines and N‐carboxy anhydrides (NCA) thereof for peptide synthesis. The S‐alkylsulfonyl group is stable against amines and thus enables its use under Fmoc chemistry conditions and the controlled polymerization

  可逆性交联蛋白质和多肽的能力使氨基酸半胱氨酸在自然界以及多肽化学中具有独特的作用。我们报告了一类新型的S-烷基磺酰基-L-半胱氨酸和N-羧基酐（NCA）用于肽合成。该小号烷基磺酰基是针对胺稳定的，因此使它的Fmoc化学条件和相应的种NCA屈服良好定义的均聚物以及嵌段共聚物的受控聚合下使用。然而，硫醇会立即与S反应-烷基磺酰基形成不对称的二硫化物。因此，我们引入了第一个反应性半胱氨酸衍生物，以在合成多肽中有效和化学选择性地形成二硫化物，从而绕开了其他保护基团的裂解步骤。
• γ-Radiolysis of Cysteine-Cysteamine Disulfide in Aqueous Solution
  作者：J. W. Purdie

  DOI：10.1139/v71-122

  日期：1971.3.1

  γ-Radiolysis of a mixed disulfide, cysteine-cysteamine disulfide, in unbuffered aqueous solution (0.3 mM) was investigated in the presence and absence of oxygen. The principal products were the thiols (cysteine and cysteamine), the corresponding sulfinic and sulfonic acids, the symmetrical disulfides (cystine and cystamine) and ammonia. Cystine and cystamine were formed in very high yields in deaerated solution; (G(CySSCy) ~ 15) but addition of oxygen reduced the yield sharply and it was inversely proportional to the oxygen concentration except at very low oxygen levels. In aerated solution G(CySSCy) = 0.8. These observations were attributed to a chain reaction which was suppressed by oxygen:[Formula: see text]In the case of proteins, it was concluded that although chain reactions between RS• radicals and protein disulfide bonds were possible, they should be inhibited by oxygen.

  在无缓冲的水溶液（0.3 mM）中研究了混合二硫键半胱氨酸-半胱酰胺二硫键的γ-辐解，同时考虑了氧气的存在和缺失。主要产物为巯基（半胱氨酸和半胱酰胺）、相应的磺酸和磺酸酐、对称二硫键（半胱氨酸和半胱酰胺）和氨。在无氧溶液中，半胱氨酸和半胱酰胺的产率很高（G(CySSCy) ~ 15），但加入氧气会显著降低产率，产率与氧气浓度成反比关系，除非氧气浓度很低。在有氧溶液中，G(CySSCy) = 0.8。这些观察结果被归因于一个被氧气抑制的链反应：[公式见原文]对于蛋白质而言，虽然RS•自由基和蛋白质二硫键之间的链反应是可能的，但应该会被氧气抑制。
• A retro-inverso TAT-like peptide designed to deliver cysteamine to cells
  作者：Jongdoo Lim、Jean-Philippe Pellois、Eric E. Simanek

  DOI：10.1016/j.bmcl.2010.07.046

  日期：2010.11

  A retro-inverso, TAT-like peptide wherein lysine residues are replaced with cysteine residues bearing a disulfide-linked cysteamine group is found to engage in thiol-disulfide exchange with cysteine. These peptides are transported into cells and localize to lysosomes. Cellular uptake is enhanced in peptides bearing two cysteamine groups over those with one or none, by factors of approximately 1.5 and 12, respectively. (C) 2010 Elsevier Ltd. All rights reserved.
• A Kinetic Approach to Characterize the Electrostatic Environments of Thiol Groups in Proteins
  作者：Hao Zhang、Min Le、Gary E. Means

  DOI：10.1006/bioo.1998.1112

  日期：1998.12

  In this study, we synthesized a zwitterionic DTNB derivative, 5-(2-aminoethyl)-dithio-2-nitrobenzoate (ADNB), and characterized its reactions with several cationic, anionic, and neutral thiols. Reactions with ADNB, unlike those with DTNB, are relatively insensitive to electrostatic environments and ionic strengths. At relatively low ionic strength, rate ratios, k(ADNB)/k(DTNB), varied from 0.22 for reactions with low-molecular-weight cationic thiols to 3.0 for those with low-molecular-weight anionic thiols. A k(ADNB)/k(DTNB) ratio of similar to 200 for Cys-34 of BSA appears to reflect a very anionic environment. k(ADNB)/k(DTNB) ratios of similar to 6 and similar to 1, respectively, for canine and equine serum albumins, which have Glu-82 -->, Asp and Glu-82 -->, Ala substitutions suggest Glu-82 is the most important anionic residues affecting the reactivity of Cys-34 in BSA. k(ADNB)/k(DTNB) ratios appear to be useful for characterizing electrostatic environments of thiol groups in proteins. (C) 1998 Academic Press.
• Of Thiols and Disulfides: Methods for Chemoselective Formation of Asymmetric Disulfides in Synthetic Peptides and Polymers
  作者：Olga Schäfer、Matthias Barz

  DOI：10.1002/chem.201800681

  日期：2018.8.22

  media to form S−C bonds, possibilities for the chemoselective formation of asymmetric disulfides have been less approached. Focusing on bioreversibility in conjugation chemistry, the formation of disulfide bonds is highly desirable for the attachment of thiol‐containing bioactive agents to proteins or in cross‐linking reactions, because disulfide bonds can combine stability in blood with degradability inside

  在蛋白质或肽化学中，硫醇经常被选作化学选择性修饰反应的化学实体。尽管这是解决在水性介质中形成半胱氨酸键的半胱氨酸和高半胱氨酸的成熟方法，但是，化学选择性形成不对称二硫键的可能性却很少。关注共轭化学中的生物可逆性，对于将含硫醇的生物活性剂连接到蛋白质或进行交联反应而言，形成二硫键是非常可取的，因为二硫键可以将血液中的稳定性与细胞内的可降解性结合在一起。在此概念文章中，重点介绍了肽和聚合物材料中掺入的巯基部分的活化基团领域中的最新方法。探索了在材料合成过程中对硫醇具有高反应性的稳定性的有利组合，其重点在于简化和防止副反应以及在二硫化物形成之前进行的其他脱保护和活化步骤。此外，突出了这种化学的应用，并展望了未来的前景。