N-(3-cyclohexylpropionyl)-L-leucine methyl ester | 345977-44-8

• 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-(3-cyclohexylpropionyl)-L-leucine methyl ester
• 英文别名: methyl (2S)-2-(3-cyclohexylpropanoylamino)-4-methylpentanoate
• CAS: 345977-44-8
• 化学式: C₁₆H₂₉NO₃
• mdl: MFCD02084221
• 分子量: 283.411
• InChiKey: DWULYEJIYJUYFK-AWEZNQCLSA-N

物化性质

• 熔点：
  175-176 °C(Solv: ethyl acetate (141-78-6); hexane (110-54-3))
• 沸点：
  411.6±18.0 °C(Predicted)
• 密度：
  0.990±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  20
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-(3-cyclohexylpropionyl)-L-leucine methyl ester 在 sodium hydroxide 、 水 作用下， 以 甲醇 为溶剂， 以97%的产率得到N-(3-cyclohexylpropionyl)-L-leucine
  参考文献：
  名称：

  Structural Basis for the Potent Calpain Inhibitory Activity of Peptidyl α-Ketoacids

  摘要：

  A series of peptidyl alpha-ketoacids and alpha-ketoesters was synthesized and studied as mu-calpain inhibitors. Docking studies revealed that the mu-calpain inhibitory activity of the compounds is influenced by hydrogen bonding interactions and the potential for ionic interaction with active site residues as well as placement of a planar N-terminal capping group into the S(3) pocket of the enzyme.

  DOI：

  10.1021/jm800182c
• 作为产物：
  描述：

  3-环己基丙酸 、 L-亮氨酸甲酯盐酸盐 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 N,N-二甲基甲酰胺 为溶剂， 以98%的产率得到N-(3-cyclohexylpropionyl)-L-leucine methyl ester
  参考文献：
  名称：

  Structural Basis for the Potent Calpain Inhibitory Activity of Peptidyl α-Ketoacids

  摘要：

  A series of peptidyl alpha-ketoacids and alpha-ketoesters was synthesized and studied as mu-calpain inhibitors. Docking studies revealed that the mu-calpain inhibitory activity of the compounds is influenced by hydrogen bonding interactions and the potential for ionic interaction with active site residues as well as placement of a planar N-terminal capping group into the S(3) pocket of the enzyme.

  DOI：

  10.1021/jm800182c

文献信息

• Structural Basis for the Potent Calpain Inhibitory Activity of Peptidyl α-Ketoacids
  作者：Isaac O. Donkor、Haregewein Assefa、Jiuyu Liu

  DOI：10.1021/jm800182c

  日期：2008.7.1

  A series of peptidyl alpha-ketoacids and alpha-ketoesters was synthesized and studied as mu-calpain inhibitors. Docking studies revealed that the mu-calpain inhibitory activity of the compounds is influenced by hydrogen bonding interactions and the potential for ionic interaction with active site residues as well as placement of a planar N-terminal capping group into the S(3) pocket of the enzyme.