(S)-5-((S)-1-azido-3-methylbutyl)dihydrofuran-2(3H)-one | 1292778-95-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酯类
• 英文名称: (S)-5-((S)-1-azido-3-methylbutyl)dihydrofuran-2(3H)-one
• 英文别名: (5S)-5-[(1S)-1-azido-3-methylbutyl]oxolan-2-one
• CAS: 1292778-95-0
• 化学式: C₉H₁₅N₃O₂
• 分子量: 197.237
• InChiKey: PLJOLGMCUVCDMY-YUMQZZPRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  14
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.89
• 拓扑面积：
  40.7
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (S)-5-((S)-1-azido-3-methylbutyl)dihydrofuran-2(3H)-one 在 4-二甲氨基吡啶 、 偶氮二异丁腈 、 palladium 10% on activated carbon 、 三苯基氢化锡 、 氢气 、 三乙胺 、 lithium diisopropyl amide 作用下， 以 四氢呋喃 、 正己烷 、 乙酸乙酯 、 甲苯 为溶剂， -78.0~110.0 ℃ 、101.33 kPa 条件下， 反应 13.33h， 生成 (2R,4S,5S)-2-(2-propyl)-4-hydroxy-5-<(tert-butyloxycarbonyl)amino>-7-methyloctanoic acid δ-lactone
  参考文献：
  名称：

  On a Possible Neutral Charge State for the Catalytic Dyad in β-Secretase When Bound to Hydroxyethylene Transition State Analogue Inhibitors

  摘要：

  beta-Secretase is one of the aspartic proteases involved in the formation of amyloid plaques in Alzheimer's disease patients Our previous results using a combination of surface plasmon resonance experiments with molecular Modeling calculations: suggested that the Asp dyad in beta-secretase bound to hydroxylethylene containing inhibitors adopts a neutral charged state. In this work, we show that the Asp dyad diprotonated state reproduced the binding ranking of a set of these inhibitors better than alternative protonation states.

  DOI：

  10.1021/jm101568y
• 作为产物：
  描述：

  (R)-3-methyl-1-((S)-5-oxotetrahydrofuran-2-yl)butyl methanesulfonate 在 sodium azide 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 12.0h， 以1.89 g的产率得到(S)-5-((S)-1-azido-3-methylbutyl)dihydrofuran-2(3H)-one
  参考文献：
  名称：

  On a Possible Neutral Charge State for the Catalytic Dyad in β-Secretase When Bound to Hydroxyethylene Transition State Analogue Inhibitors

  摘要：

  beta-Secretase is one of the aspartic proteases involved in the formation of amyloid plaques in Alzheimer's disease patients Our previous results using a combination of surface plasmon resonance experiments with molecular Modeling calculations: suggested that the Asp dyad in beta-secretase bound to hydroxylethylene containing inhibitors adopts a neutral charged state. In this work, we show that the Asp dyad diprotonated state reproduced the binding ranking of a set of these inhibitors better than alternative protonation states.

  DOI：

  10.1021/jm101568y

文献信息

• On a Possible Neutral Charge State for the Catalytic Dyad in β-Secretase When Bound to Hydroxyethylene Transition State Analogue Inhibitors
  作者：Fredy Sussman、José M. Otero、M. Carmen Villaverde、Marian Castro、José L. Domínguez、Lucía González-Louro、Ramón J. Estévez、J. Carlos Estévez

  DOI：10.1021/jm101568y

  日期：2011.4.28

  beta-Secretase is one of the aspartic proteases involved in the formation of amyloid plaques in Alzheimer's disease patients Our previous results using a combination of surface plasmon resonance experiments with molecular Modeling calculations: suggested that the Asp dyad in beta-secretase bound to hydroxylethylene containing inhibitors adopts a neutral charged state. In this work, we show that the Asp dyad diprotonated state reproduced the binding ranking of a set of these inhibitors better than alternative protonation states.