半胱氨酸-谷胱甘肽二硫醚 | 13081-14-6

• 物质功能分类: 生物化工 - 氨基酸及其衍生物 - 半胱氨酸类衍生物
• 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
• 中文名称: 半胱氨酸-谷胱甘肽二硫醚
• 中文别名: L-半胱氨酸；L -半胱氨酸
• 英文名称: N⁵-((R)-3-(((R)-2-amino-2-carboxyethyl)disulfanyl)-1-((carboxymethyl)amino)-1-oxopropan-2-yl)-L-glutamine
• 英文别名: N-<3-<(2-amino-2-carboxyethyl)dithio>-N-L-γ-glutamyl-L-alanyl>glycine；L-cysteine-glutathione disulfide；γ-L-Glutamyl-L-cysteinyl-S-(S-L-cystein)-glycin；S-Glutathionyl-L-cysteine；(2S)-2-amino-5-[[(2R)-3-[[(2R)-2-amino-2-carboxyethyl]disulfanyl]-1-(carboxymethylamino)-1-oxopropan-2-yl]amino]-5-oxopentanoic acid
• CAS: 13081-14-6
• 化学式: C₁₃H₂₂N₄O₈S₂
• 分子量: 426.472
• InChiKey: BNRXZEPOHPEEAS-FXQIFTODSA-N

物化性质

• 熔点：
  234(dec.)
• 沸点：
  882.0±65.0 °C(Predicted)
• 密度：
  1.549±0.06 g/cm3(Predicted)
• 溶解度：
  可溶于水基（轻微），水（轻微，加热）

计算性质

• 辛醇/水分配系数(LogP)：
  -7.7
• 重原子数：
  27
• 可旋转键数：
  14
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  273
• 氢给体数：
  7
• 氢受体数：
  12

安全信息

• 危险品标志：
  Xi

反应信息

• 作为反应物：
  描述：

  L-半胱氨酸 、 半胱氨酸-谷胱甘肽二硫醚 在 sodium chloride 作用下， 以 重水 为溶剂， 生成 L-胱氨酸 、 谷胱甘肽
  参考文献：
  名称：

  Kinetics and equilibria of thiol/disulfide interchange reactions of selected biological thiols and related molecules with oxidized glutathione

  摘要：

  Rate constants for reaction of coenzyme A and cysteine with oxidized glutathione (GSSG) and equilibrium constants for the reaction of coenzyme A, cysteine, homocysteine, cysteamine, and related thiols with GSSG by thiol/disulfide interchange were determined over a range of pD values by NMR spectroscopy. The rate constants for reaction of the thiolate anion forms of coenzyme A and cysteine with GSSG suggest that reduction of GSSG by coenzyme A and cysteine is a mechanistically uncomplicated S(N)2 reaction. Equilibrium constants for the thiol/disulfide interchange reactions show a strong dependence on the Bronsted basicity of the thiolate anion. In a similar way, DELTA-E-degrees', the difference between the half-cell potentials for the RSSR/RSH and GSSG/GSH redox couples, is linearly dependent on the difference between the pK(A) values of RSH and glutathione: DELTA-E-degrees' = 64-DELTA-pK(A) -7.7 where DELTA-E-degrees' is in units of mV. The reducing strength at a given pH is also determined by the fraction of the thiol present in the reactive thiolate form. At pD 7, the half-cell potentials for coenzyme A, cysteine, homocysteine, and cysteamine are close to that of glutathione, the major intracellular thiol redox system, which suggests that small changes in the intracellular redox potential can cause significant changes in the intracellular distribution of these biological thiols between their reduced and oxidized forms.

  DOI：

  10.1021/jo00027a023
• 作为产物：
  描述：

  N-(N-L-γ-谷氨酰基-S-亚硝基-L-半胱氨酰----甘氨酸 在 盐酸 、 碳酸氢钠 作用下， 以 水 为溶剂， 反应 21.0h， 生成 半胱氨酸-谷胱甘肽二硫醚
  参考文献：
  名称：

  Triolsulphonate derivatives of amino acids

  摘要：

  DOI：

  10.1016/s0040-4039(00)89276-x

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。
• 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。
• Reactions of cysteine sulfenyl thiocyanate with thiols to give unsymmetrical disulfides
  作者：Susan L. Alguindigue Nimmo、Kelemu Lemma、Michael T. Ashby

  DOI：10.1002/hc.20340

  日期：2007.7

  Cysteine sulfenyl thiocyanate (CSSCN) reacts with thiols at pH 0 to cleanly yield disulfides. 2-Mercaptoethanol (2-MESH), 3-mercaptopropionic acid (3-MPASH), penicillamine (PENSH), and glutathione (GSH) react with CSSCN to give the corresponding mixed disulfides: 2-MESSC, 3-MPASSC, PENSSC, and GSSC. These compounds are stable at pH 0 and have been characterized by 1H and 13C NMR spectroscopy. © 2007

  半胱氨酸硫氰酸亚硫基酯 (CSSCN) 在 pH 值为 0 时与硫醇反应，干净地生成二硫化物。2-巯基乙醇 (2-MESH)、3-巯基丙酸 (3-MPASH)、青霉胺 (PENSH) 和谷胱甘肽 (GSH) 与 CSSCN 反应生成相应的混合二硫化物：2-MESSC、3-MPASSC、PENSSC 和GSSC。这些化合物在 pH 值为 0 时稳定，并已通过 1H 和 13C NMR 光谱进行表征。© 2007 Wiley Periodicals, Inc. 18:467–471, 2007；在线发表于 Wiley InterScience (www.interscience.wiley.com)。DOI 10.1002/hc.20340
• Conversion of S-phenylsulfonylcysteine residues to mixed disulfides at pH 4.0: utility in protein thiol blocking and in protein-S-nitrosothiol detection
  作者：B. D. Reeves、N. Joshi、G. C. Campanello、J. K. Hilmer、L. Chetia、J. A. Vance、J. N. Reinschmidt、C. G. Miller、D. P. Giedroc、E. A. Dratz、D. J. Singel、P. A. Grieco

  DOI：10.1039/c4ob00995a

  日期：——

  A protocol denoted as the thiosulfonate switch featuring sequential protein thiol blocking and conversion of protein-S-nitrosothiols to mixed disulfides bearing a fluorescent probe at pH 4.0 is reported.

  一种被称为硫代亚砜开关的协议，其特点是在pH 4.0下，依次阻断蛋白质巯基并将蛋白质-S-亚硝基硫醇转化为带有荧光探针的混合二硫化物。
• Characterization of the disulfides of bio-thiols by electrospray ionization and triple-quadrupole tandem mass spectrometry
  作者：Federico Maria Rubino、Cinzia Verduci、Rosario Giampiccolo、Salvatore Pulvirenti、Gabri Brambilla、Antonio Colombi

  DOI：10.1002/jms.745

  日期：2004.12

  Glutathione and other intracellular low molecular mass thiols act both as the major endogenous antioxidant and redox buffer system and, as recently highlighted, as an important regulator of cellular homeostasis. Such cellular functions are mediated by protein thiolation, a newly recognized post-translational modification which involves the formation of mixed disulfides between GSH and key disulfide-linked Cys residues in the native protein structure. It is also well known that thiol-seeking heavy metals, such as mercury, cadmium and lead, may interfere in this regulatory system, thus disrupting the cellular functioning. To identify such mixed disulfides in order to investigate their biological role, 15 homo- and heterodimeric disulfides were prepared by air oxidation of binary mixtures containing cysteine, homocysteine, penicillamine, N-acetylcysteine, N-acetylpenicillamine and glutathione and their protonated molecules were characterized by mass spectrometry. Collisionally activated unimolecular decomposition of protonated homo- and heterodimeric disulfides generated by electrospray ionization gives rise to fission of the disulfide system both between the two sulfur atoms and across the CS bonds, to yield structurally specific fragments which allow one to define the structure of the compounds and to discriminate between isomeric compounds. Fission between the sulfur atoms yields a pair of RS+ ions and, in some cases, also the complementary fragments corresponding to the protonated amino acids. Fission across the CS bonds mainly occurs in the disulfides of N-acetylcysteine and N-acetylpenicillamine and gives rise to non-S-containing fragments formally similar to those obtained from some mercapturic acids. The complementary fragments, formally connected as RSS+ ions are also observed. Fragmentation of glutathione disulfides mainly shows the characteristic loss of the terminal γ-linked glutamic acid and little, if any, fragmentation of the disulfide system. Copyright © 2004 John Wiley & Sons, Ltd.

  谷胱甘肽和其他细胞内低分子量硫醇既是主要的内源性抗氧化剂和氧化还原缓冲系统，也正如最近强调的那样，是细胞稳态的重要调节因子。这种细胞功能的介导依赖于蛋白质硫化，这是一种新识别的翻译后修饰，涉及谷胱甘肽与本征蛋白结构中关键的二硫键连接的半胱氨酸残基之间形成混合二硫化物。众所周知，寻硫重金属如汞、镉和铅可能干扰这一调节系统，从而破坏细胞功能。为了鉴定这些混合二硫化物以探讨它们的生物学作用，通过空气氧化含有半胱氨酸、同型半胱氨酸、青霉胺、N-乙酰半胱氨酸、N-乙酰青霉胺和谷胱甘肽的二元混合物，制备了15种同二聚体和异二聚体二硫化物，并通过质谱对其质子化分子进行了表征。通过电喷雾电离生成的质子化同二聚体和异二聚体二硫化物发生碰撞激活的单分子解离，引发二硫化物系统在两个硫原子之间及CS键上的裂解，产生结构特异的片段，这些片段可以用来确定化合物的结构并区分异构化合物。硫原子之间的裂解产生一对RS+离子，在某些情况下，还会产生与质子化氨基酸对应的互补片段。CS键的裂解主要发生在N-乙酰半胱氨酸和N-乙酰青霉胺的二硫化物中，并产生在形式上类似于一些巯基酸获得的非S含 Fragment。互补片段在形式上连接为RSS+离子也被观察到。谷胱甘肽二硫化物的裂解主要显示终端γ-连接的谷氨酸的特征性损失，几乎没有或很少有二硫化物系统的裂解。版权 © 2004 John Wiley & Sons, Ltd.