N-((1S)-1-{[(4-hydroxyphenyl)amino]methyl}propyl)-N2-[(morpholin-4-yl)carbonyl]-L-leucinamide | 757976-49-1

• 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-((1S)-1-{[(4-hydroxyphenyl)amino]methyl}propyl)-N2-[(morpholin-4-yl)carbonyl]-L-leucinamide
• 英文别名: N-((1S)-1-{[(4-hydroxyphenyl)amino]methyl}propyl)-N²-[(morpholin-4-yl)carbonyl]-L-leucinamide
• CAS: 757976-49-1
• 化学式: C₂₁H₃₄N₄O₄
• 分子量: 406.525
• InChiKey: KFJXBWMMULSUNC-LPHOPBHVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.16
• 重原子数：
  29.0
• 可旋转键数：
  9.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  102.93
• 氢给体数：
  4.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  N-((1S)-1-{[(4-hydroxyphenyl)amino]methyl}propyl)-N2-[(morpholin-4-yl)carbonyl]-L-leucinamide 在 sodium hydride 、 三氟乙酸 作用下， 以 四氢呋喃 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 3.0h， 生成 {4-[((2S)-2-{[N-(morpholin-4-ylcarbonyl)-L-leucyl]amino}butyl)amino]phenoxy}acetic acid
  参考文献：
  名称：

  Arylamine based cathepsin K inhibitors: Investigating P3 heterocyclic substituents

  摘要：

  A modification of novel cathepsin K inhibitors I was carried out. The structural design was aimed at reducing the lipophilic character of compounds I for obtaining better pharmacokinetic profiles. This modification afforded several less lipophilic compounds with good inhibitory activities and pharmacokinetic profiles, although the enzyme selectivity over cathepsin S was left at issue. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2006.06.031
• 作为产物：
  描述：

  L-亮氨酸苄酯对甲苯磺酸盐 在 palladium on activated charcoal 氢气 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 作用下， 以 乙醇 、 二氯甲烷 为溶剂， 反应 33.0h， 生成 N-((1S)-1-{[(4-hydroxyphenyl)amino]methyl}propyl)-N2-[(morpholin-4-yl)carbonyl]-L-leucinamide
  参考文献：
  名称：

  Arylamine based cathepsin K inhibitors: Investigating P3 heterocyclic substituents

  摘要：

  A modification of novel cathepsin K inhibitors I was carried out. The structural design was aimed at reducing the lipophilic character of compounds I for obtaining better pharmacokinetic profiles. This modification afforded several less lipophilic compounds with good inhibitory activities and pharmacokinetic profiles, although the enzyme selectivity over cathepsin S was left at issue. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2006.06.031