[2-(2,3-Dihydro-1,4-benzodioxin-6-yl)ethyl]thiourea | 1152583-31-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并二恶烷
• 英文名称: [2-(2,3-Dihydro-1,4-benzodioxin-6-yl)ethyl]thiourea
• 英文别名: 2-(2,3-dihydro-1,4-benzodioxin-6-yl)ethylthiourea
• CAS: 1152583-31-7
• 化学式: C₁₁H₁₄N₂O₂S
• mdl: MFCD10690399
• 分子量: 238.31
• InChiKey: ALWBFAIIQWRRFZ-UHFFFAOYSA-N

物化性质

• 沸点：
  402.7±55.0 °C(Predicted)
• 密度：
  1.287±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.4
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.363
• 拓扑面积：
  88.6
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  [2-(2,3-Dihydro-1,4-benzodioxin-6-yl)ethyl]thiourea 、 氰乙酸乙酯 在 乙醇 、 sodium ethanolate 作用下， 反应 4.0h， 以42%的产率得到6-Amino-1-[2-(2,3-dihydro-1,4-benzodioxin-6-yl)ethyl]-2-sulfanylidenepyrimidin-4-one
  参考文献：
  名称：

  Evaluation of 2-thioxo-2,3,5,6,7,8-hexahydropyrimido[4,5-d]pyrimidin-4(1H)-one analogues as GAA activators

  摘要：

  Pompe disease is a lysosomal storage disease (LSD) caused by a deficiency in the lysosomal enzyme acid alpha-glucosidase. In several LSDs, enzyme inhibitors have been used as small molecule chaperones to facilitate and increase the translocation of mutant protein from the endoplasmic reticulum to the lysosome. Enzyme activators with chaperone activity would be even more desirable as they would not inhibit the enzyme after translocation and might potentiate the activity of the enzyme that is successfully translocated. Herein we report our initial findings of a new series of acid alpha-glucosidase activators. Published by Elsevier Masson SAS.

  DOI：

  10.1016/j.ejmech.2010.01.027
• 作为产物：
  描述：

  硫氰酸铵 、 2-(2,3-二氢-1,4-苯并二氧杂环己-6-基)乙胺盐酸盐 以 溴苯 为溶剂， 以20%的产率得到[2-(2,3-Dihydro-1,4-benzodioxin-6-yl)ethyl]thiourea
  参考文献：
  名称：

  Evaluation of 2-thioxo-2,3,5,6,7,8-hexahydropyrimido[4,5-d]pyrimidin-4(1H)-one analogues as GAA activators

  摘要：

  Pompe disease is a lysosomal storage disease (LSD) caused by a deficiency in the lysosomal enzyme acid alpha-glucosidase. In several LSDs, enzyme inhibitors have been used as small molecule chaperones to facilitate and increase the translocation of mutant protein from the endoplasmic reticulum to the lysosome. Enzyme activators with chaperone activity would be even more desirable as they would not inhibit the enzyme after translocation and might potentiate the activity of the enzyme that is successfully translocated. Herein we report our initial findings of a new series of acid alpha-glucosidase activators. Published by Elsevier Masson SAS.

  DOI：

  10.1016/j.ejmech.2010.01.027