(S)-5-((R)-1-hydroxy-3-methylbutyl)dihydrofuran-2(3H)-one | 1292778-94-9

• 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-((R)-1-hydroxy-3-methylbutyl)dihydrofuran-2(3H)-one
• 英文别名: (5S)-5-[(1R)-1-hydroxy-3-methylbutyl]oxolan-2-one
• CAS: 1292778-94-9
• 化学式: C₉H₁₆O₃
• 分子量: 172.224
• InChiKey: NEHAVLOJIYHTHF-SFYZADRCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  12
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.89
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (S)-5-((R)-1-hydroxy-3-methylbutyl)dihydrofuran-2(3H)-one 在 吡啶 、 4-二甲氨基吡啶 、 sodium azide 、 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 、 N,N-二甲基甲酰胺 、 甲苯 为溶剂， -78.0~110.0 ℃ 、101.33 kPa 条件下， 反应 30.33h， 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：

  (5S,1'S)-5-(2'-bromo-1'-hydroxy)ethyl-4,5-dihydro-2-(3H)-furanone 在 potassium carbonate 、 lithium chloride 、 copper dichloride 作用下， 以 四氢呋喃 、 乙醚 、 丙酮 为溶剂， 反应 20.5h， 生成 (S)-5-((R)-1-hydroxy-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.