2-[2-octadecyloxyethoxy]ethanethiol | 1025999-17-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-[2-octadecyloxyethoxy]ethanethiol
• 英文别名: 2-(2-Octadecoxyethoxy)ethanethiol
• CAS: 1025999-17-0
• 化学式: C₂₂H₄₆O₂S
• 分子量: 374.672
• InChiKey: GZTWMVBPQIQFQG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.2
• 重原子数：
  25
• 可旋转键数：
  22
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  19.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-[2-octadecyloxyethoxy]ethanethiol 在 碘 、 三苯基膦 作用下， 以 苯 为溶剂， 反应 12.0h， 以66%的产率得到1-[2-(2-iodoethoxy)ethoxy]octadecane
  参考文献：
  名称：

  Efficient Synthesis of Methanesulphonate-Derived Lipid Chains for Attachment of Proteins to Lipid Membranes

  摘要：

  We have developed an easy and flexible synthetic methodology to obtain lipid chains containing methanothiosulfonate terminal groups with the aim to attach them to natural proteins as functional groups. There are many proteins found in nature that are modified by lipids, and this is a key part of their function. For example, the prion protein is attached to the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor, and this protein is thought to be the causative agent in diseases such as bovine spongiform encephalopathy (BSE; mad cow disease) and the human equivalent Creutzfeldt-Jakob disease. However, production of large amounts of protein in bacteria results in proteins that lack these lipid modifications. The lipid chains containing methanothiosulfonate terminal groups that we have synthesized here can be attached to these proteins through the thiol contained in the side chain of the cysteine residue, which can be incorporated into the protein sequence at the desired position.

  DOI：

  10.1080/00397910802213794
• 作为产物：
  描述：

  [2-(2-octadecyloxyethoxy)ethylsulfanylmethyl]benzene 在 氨 、 sodium 作用下， 以 四氢呋喃 为溶剂， 反应 3.0h， 以74%的产率得到2-[2-octadecyloxyethoxy]ethanethiol
  参考文献：
  名称：

  Carbohydrate–protein interactions at interfaces: synthesis of thiolactosyl glycolipids and design of a working model for surface plasmon resonance

  摘要：

  用于碳水化合物-蛋白质结合研究的硫代半乳糖脂已经合成。其中一种代表被选用于与植物凝集素RCA120（蓖麻的凝集素）结合的研究。使用BIAcore表面等离子共振仪器实时定量测量了相互作用。用β-半乳糖苷酶从硫代半乳糖脂中原位去除大部分半乳糖表明凝集素结合具有高度特异性。1-{2-[2-(2-[β-D-半乳糖基-(1 → 4)-1-硫代-β-D-吡喃葡萄糖基]乙氧基)乙氧基]乙氧基}十八烷30的解离常数KD=8.77×10-8 M，比溶液中与乳糖结合的解离常数高四个数量级。需要浓度大于80mM的乳糖才能阻止凝集素与新膜中的硫代半乳糖脂结合。

  DOI：

  10.1039/b210672h

文献信息

• Carbohydrate–protein interactions at interfaces: synthesis of thiolactosyl glycolipids and design of a working model for surface plasmon resonance
  作者：Peter Critchley、M. Nicolas Willand、Atvinder K. Rullay、David H. G. Crout

  DOI：10.1039/b210672h

  日期：2003.3.13

  Thiolactosyl lipids designed for carbohydrate-protein binding studies have been synthesised. One representative was selected for binding studies with a plant lectin RCA120, the agglutinin from Ricinus communis. The interactions were measured quantitatively in real time using a BIAcore surface plasmon resonance instrument. Removal of much of the galactose from the thiolactosyl lipid in situ with β-galactosidase showed that the lectin binding was highly specific. A dissociation constant KD = 8.77 × 10−8 M was measured for 1-2-[2-(2-[β-D-galactopyranosyl-(1 → 4)-1-thio-β-D-glucopyranosyl]ethoxy)ethoxy]ethoxy}octadecane 30 which is four orders of magnitude greater than that determined for binding to lactose in solution. A concentration of lactose of >80 mM was required to block the lectin binding to thiolactosyl lipid in a neomembrane.

  用于碳水化合物-蛋白质结合研究的硫代半乳糖脂已经合成。其中一种代表被选用于与植物凝集素RCA120（蓖麻的凝集素）结合的研究。使用BIAcore表面等离子共振仪器实时定量测量了相互作用。用β-半乳糖苷酶从硫代半乳糖脂中原位去除大部分半乳糖表明凝集素结合具有高度特异性。1-2-[2-(2-[β-D-半乳糖基-(1 → 4)-1-硫代-β-D-吡喃葡萄糖基]乙氧基)乙氧基]乙氧基}十八烷30的解离常数KD=8.77×10-8 M，比溶液中与乳糖结合的解离常数高四个数量级。需要浓度大于80mM的乳糖才能阻止凝集素与新膜中的硫代半乳糖脂结合。
• Efficient Synthesis of Methanesulphonate-Derived Lipid Chains for Attachment of Proteins to Lipid Membranes
  作者：Matthew R. Hicks、Atvinder K. Rullay、Rosa Pedrido、David H. Crout、Teresa J. T. Pinheiro

  DOI：10.1080/00397910802213794

  日期：2008.10.22

  We have developed an easy and flexible synthetic methodology to obtain lipid chains containing methanothiosulfonate terminal groups with the aim to attach them to natural proteins as functional groups. There are many proteins found in nature that are modified by lipids, and this is a key part of their function. For example, the prion protein is attached to the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor, and this protein is thought to be the causative agent in diseases such as bovine spongiform encephalopathy (BSE; mad cow disease) and the human equivalent Creutzfeldt-Jakob disease. However, production of large amounts of protein in bacteria results in proteins that lack these lipid modifications. The lipid chains containing methanothiosulfonate terminal groups that we have synthesized here can be attached to these proteins through the thiol contained in the side chain of the cysteine residue, which can be incorporated into the protein sequence at the desired position.