N-<(4-methylpiperazin-1-yl)carbonyl>cyclohexylalanine | 147984-25-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: N-<(4-methylpiperazin-1-yl)carbonyl>cyclohexylalanine
• 英文别名: (2S)-3-cyclohexyl-2-[(4-methylpiperazine-1-carbonyl)amino]propanoic acid
• CAS: 147984-25-6
• 化学式: C₁₅H₂₇N₃O₃
• 分子量: 297.398
• InChiKey: XIEVFVRAEAXYMZ-ZDUSSCGKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  21
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.87
• 拓扑面积：
  72.9
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-<(4-methylpiperazin-1-yl)carbonyl>cyclohexylalanine 、 N-<(2S,3R,4S)-1-(2-naphthyl)-3,4-dihydroxy-6-methyl-2-heptyl>Ile-NH2 在 N-甲基吗啉 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 生成 (2S,3R,4S)-2-cyclohexylalanylisoleucyl>amino>-1-(2-naphthyl)-3,4-dihydroxy-6-methylheptane
  参考文献：
  名称：

  Potent and selective inhibitors of an aspartyl protease-like endothelin converting enzyme identified in rat lung

  摘要：

  Two structurally distinct series of potent and selective inhibitors of an aspartyl protease-like endothelin converting enzyme (ECE) activity identified in the rat lung have been developed. Pepstatin A, which potently inhibits the rat lung ECE, served as the basis for the first series. Alternatively, selected renin inhibitors containing the dihydroxyethylene moiety were shown to be inhibitors of rat lung activity. Subsequent modifications improved inhibition of the rat lung ECE while eliminating renin activity. Both series of ECE inhibitors demonstrated a range of selectivity over Cathepsin D. Water-solubilizing moieties were appended onto selected compounds to facilitate in vivo testing. Partial reduction of the pressor response to exogenously administered Big ET-1 was observed with selected rat lung ECE inhibitors.

  DOI：

  10.1021/jm00056a007
• 作为产物：
  描述：

  L-环己基丙氨酸甲酯盐酸盐 在 lithium hydroxide 作用下， 以 四氢呋喃 、 二氯甲烷 、 甲苯 为溶剂， 反应 5.5h， 生成 N-<(4-methylpiperazin-1-yl)carbonyl>cyclohexylalanine
  参考文献：
  名称：

  Potent and selective inhibitors of an aspartyl protease-like endothelin converting enzyme identified in rat lung

  摘要：

  Two structurally distinct series of potent and selective inhibitors of an aspartyl protease-like endothelin converting enzyme (ECE) activity identified in the rat lung have been developed. Pepstatin A, which potently inhibits the rat lung ECE, served as the basis for the first series. Alternatively, selected renin inhibitors containing the dihydroxyethylene moiety were shown to be inhibitors of rat lung activity. Subsequent modifications improved inhibition of the rat lung ECE while eliminating renin activity. Both series of ECE inhibitors demonstrated a range of selectivity over Cathepsin D. Water-solubilizing moieties were appended onto selected compounds to facilitate in vivo testing. Partial reduction of the pressor response to exogenously administered Big ET-1 was observed with selected rat lung ECE inhibitors.

  DOI：

  10.1021/jm00056a007