diethyl [4-(acetylthio)phenyl]methylphosphonate | 1025505-66-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯硫酚酯
• 英文名称: diethyl [4-(acetylthio)phenyl]methylphosphonate
• CAS: 1025505-66-1
• 化学式: C₁₃H₁₉O₄PS
• 分子量: 302.331
• InChiKey: RXPKEXAOKHXQPM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.09
• 重原子数：
  19.0
• 可旋转键数：
  7.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  52.6
• 氢给体数：
  0.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  diethyl [4-(acetylthio)phenyl]methylphosphonate 在 盐酸 作用下， 反应 5.0h， 以83%的产率得到(4-mercaptophenyl)methylphosphonic acid
  参考文献：
  名称：

  Rate enhancement of the oxidative folding of lysozyme by the use of aromatic thiol containing redox buffers

  摘要：

  Almost all therapeutic proteins and most extracellular proteins contain disulfide bonds. The production of these proteins in bacteria or in vitro is challenging due to the need to form the correctly matched disulfide bonds during folding. One important parameter for efficient in vitro folding is the composition of the redox buffer, a mixture of a small molecule thiol and small molecule disulfide. The effects of different redox buffers on protein folding, however, have received limited attention. The oxidative folding of denatured reduced lysozyme was followed in the presence of redox buffers containing varying concentrations of five different aromatic thiols or the traditional aliphatic thiol glutathione (GSH). Aromatic thiols eliminated the lag phase at low disulfide concentrations, increased the folding rate constant up to 11-fold, and improved the yield of active protein relative to GSH. The yield of active protein was similar for four of the five aromatic thiols and for glutathione at pH 7 as well as for glutathione at pH 8.2. At pH 6 the positively charged aromatic thiol provided a higher yield than the negatively charged thiols. (C) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2007.11.047
• 作为产物：
  描述：

  diethyl [4-(benzoylthio)phenyl]methylphosphonate 、 乙酸酐 在 sodium ethanolate 作用下， 以 乙醇 为溶剂， 反应 0.42h， 以96%的产率得到diethyl [4-(acetylthio)phenyl]methylphosphonate
  参考文献：
  名称：

  Rate enhancement of the oxidative folding of lysozyme by the use of aromatic thiol containing redox buffers

  摘要：

  Almost all therapeutic proteins and most extracellular proteins contain disulfide bonds. The production of these proteins in bacteria or in vitro is challenging due to the need to form the correctly matched disulfide bonds during folding. One important parameter for efficient in vitro folding is the composition of the redox buffer, a mixture of a small molecule thiol and small molecule disulfide. The effects of different redox buffers on protein folding, however, have received limited attention. The oxidative folding of denatured reduced lysozyme was followed in the presence of redox buffers containing varying concentrations of five different aromatic thiols or the traditional aliphatic thiol glutathione (GSH). Aromatic thiols eliminated the lag phase at low disulfide concentrations, increased the folding rate constant up to 11-fold, and improved the yield of active protein relative to GSH. The yield of active protein was similar for four of the five aromatic thiols and for glutathione at pH 7 as well as for glutathione at pH 8.2. At pH 6 the positively charged aromatic thiol provided a higher yield than the negatively charged thiols. (C) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2007.11.047