N⁶-α-Lipoyl-L-lysin | 1676-89-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二硫杂环戊烷
• 英文名称: N⁶-α-Lipoyl-L-lysin
• 英文别名: N(6)-lipoyl-L-lysine；(2S)-2-amino-6-[5-(dithiolan-3-yl)pentanoylamino]hexanoic acid
• CAS: 1676-89-7
• 化学式: C₁₄H₂₆N₂O₃S₂
• 分子量: 334.504
• InChiKey: COTIXRRJLCSLLS-KIYNQFGBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.1
• 重原子数：
  21
• 可旋转键数：
  11
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.86
• 拓扑面积：
  143
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N⁶-α-Lipoyl-L-lysin 在 sodium hydroxide 、 sodium tetrahydroborate 作用下， 生成 N^ε-α-Lipoyl-L-lysin
  参考文献：
  名称：

  Synthesis of Some N-Lipoyl Amino Acids and Peptides

  摘要：

  DOI：

  10.1021/ja00863a031
• 作为产物：
  描述：

  L-赖氨酸 在 氯甲酸乙酯 、 三乙胺 、 sodium hydroxide 、 copper(II) sulfate 、 硫化氢 作用下， 以 乙腈 、 水 、 溶剂黄146 为溶剂， 生成 N⁶-α-Lipoyl-L-lysin
  参考文献：
  名称：

  EP1547590

  摘要：

  公开号：

文献信息

• Site-specific protein modification by genetic encoded disulfide compatible thiols
  作者：Xinyu Ling、Heqi Chen、Wei Zheng、Liying Chang、Yong Wang、Tao Liu

  DOI：10.1016/j.cclet.2019.04.075

  日期：2020.1

  convenient way for site-specific protein modification. However, recombinant expression of disulfide bonding containing protein with unpaired cysteine is technically challenging and the resulting protein often suffers from significantly reduced yield and activity. Here we used genetic code expansion technique to introduce a surface exposed self-paired di-thiol functional group into proteins, which can be

  摘要半胱氨酸化学提供了一种低成本且方便的位点特异性蛋白质修饰方法。然而，含二硫键的蛋白质与未配对的半胱氨酸的重组表达在技术上具有挑战性，并且所得蛋白质经常遭受产量和活性显着降低的困扰。在这里，我们使用遗传密码扩展技术将表面暴露的自配对二硫醇官能团引入蛋白质中，该蛋白质可以被选择性还原以提供活性硫醇。合成了包含自配对二硫键的两种化合物，并使用绿色荧光蛋白（GFP）验证了它们的遗传掺入。使用抗体片段证明了这些自配对的二硫醇与天然二硫键的相容性，以提供位点特异性标记的抗体。
• Reed et al., Journal of Biological Chemistry, 1958, vol. 232, p. 143,144
  作者：Reed et al.

  DOI：——

  日期：——
• Nawa et al., Journal of the American Chemical Society, 1959, vol. 81, p. 2908,2909
  作者：Nawa et al.

  DOI：——

  日期：——
• Role of Lipoylation of the Immunodominant Epitope of Pyruvate Dehydrogenase Complex: Toward a Peptide-Based Diagnostic Assay for Primary Biliary Cirrhosis
  作者：Giulia Pacini、Alfonso Carotenuto、Cedric Rentier、Francesca Nuti、Feliciana Real-Fernandez、Diego Brancaccio、Giuseppina Sabatino、Maud Larregola、Elisa Peroni、Paola Migliorini、Ettore Novellino、Pier Maria Battezzati、Carlo Selmi、Anna Maria Papini、Paolo Rovero

  DOI：10.1021/acs.jmedchem.5b00783

  日期：2015.8.27

  Primary biliary cirrhosis is an immune-mediated chronic liver disease whose diagnosis relies on the detection of serum antimitochondrial antibodies directed against a complex set of proteins, among which pyruvate dehydrogenase complex is considered the main autoantigen. We studied the immunological role of the lipoyl domain of this protein using synthetic lipoylated peptides, showing that the lipoyl chain chirality does not affect autoantibody recognition and, most importantly, confirming that both lipoylated and unlipoylated peptides are able to recognize specific autoantibodies in patients sera. In fact, 74% of patients sera recognize at least one of the tested peptides but very few positive sera recognized exclusively the lipoylated peptide, suggesting that the lipoamide moiety plays a marginal role within the autoreactive epitope. These results are supported by a conformational analysis showing that the lipoyl moiety of pyruvate dehydrogenase complex appears to be involved in hydrophobic interactions, which may limit its exposition and thus its contribution to the complex antigenic epitope. A preliminary analysis of the specificity of the two most active peptides indicates that they could be part of a panel of synthetic antigens collectively able to mimic in a simple immunoenzymatic assay the complex positivity pattern detected in immunofluorescence.

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