(S)-3-(1-benzyl-2,2-dimethoxyethyl)-1-piperidin-1-ylurea | 1450733-39-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (S)-3-(1-benzyl-2,2-dimethoxyethyl)-1-piperidin-1-ylurea
• CAS: 1450733-39-7
• 化学式: C₁₇H₂₇N₃O₃
• 分子量: 321.42
• InChiKey: LMSWBUXTQJGZIQ-HNNXBMFYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.92
• 重原子数：
  23.0
• 可旋转键数：
  7.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  62.83
• 氢给体数：
  2.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  (S)-3-(1-benzyl-2,2-dimethoxyethyl)-1-piperidin-1-ylurea 在 三甲基氯硅烷 、 sodium hydride 、 sodium iodide 作用下， 以 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 49.5h， 生成 (S)-1-benzyl-3-(1-benzyl-2-oxoethyl)-1-piperidin-1-ylurea
  参考文献：
  名称：

  Modular construction of quaternary hemiaminal-based inhibitor candidates and their in cellulo assessment with HIV-1 protease

  摘要：

  Non-peptidomimetic drug-like protease inhibitors have potential for circumventing drug resistance. We developed a much-improved synthetic route to our previously reported inhibitor candidate displaying an unusual quaternized hemi-aminal. This functional group forms from a linear precursor upon passage into physiological media. Seven variants were prepared and tested in cellulo with our HIV-1 fusion-protein technology that result in an eGFP-based fluorescent readout. Three candidates showed inhibition potency above 20 mu M and toxicity at higher concentrations, making them attractive targets for further refinement. Importantly, our class of original inhibitor candidates is not recognized by two major multidrug resistance pumps, quite in contrast to most clinically applied HIV-1 protease inhibitors. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.06.018
• 作为产物：
  描述：

  (S)-(1-benzyl-2,2-dimethoxyethyl)carbamic acid benzyl ester 在 5%-palladium/activated carbon 、 氢气 、 碘甲烷 作用下， 以 四氢呋喃 、 甲醇 、 乙腈 为溶剂， 反应 39.5h， 生成 (S)-3-(1-benzyl-2,2-dimethoxyethyl)-1-piperidin-1-ylurea
  参考文献：
  名称：

  Modular construction of quaternary hemiaminal-based inhibitor candidates and their in cellulo assessment with HIV-1 protease

  摘要：

  Non-peptidomimetic drug-like protease inhibitors have potential for circumventing drug resistance. We developed a much-improved synthetic route to our previously reported inhibitor candidate displaying an unusual quaternized hemi-aminal. This functional group forms from a linear precursor upon passage into physiological media. Seven variants were prepared and tested in cellulo with our HIV-1 fusion-protein technology that result in an eGFP-based fluorescent readout. Three candidates showed inhibition potency above 20 mu M and toxicity at higher concentrations, making them attractive targets for further refinement. Importantly, our class of original inhibitor candidates is not recognized by two major multidrug resistance pumps, quite in contrast to most clinically applied HIV-1 protease inhibitors. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.06.018