N-(4-(4-fluorophenyl)-5-((Z)-2-((2S,4R)-4-hydroxy-6-oxotetrahydro-2H-pyran-2-yl)vinyl)-6-isopropylpyrimidin-2-yl)-N-methylmethanesulfonamide | 1444772-05-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: N-(4-(4-fluorophenyl)-5-((Z)-2-((2S,4R)-4-hydroxy-6-oxotetrahydro-2H-pyran-2-yl)vinyl)-6-isopropylpyrimidin-2-yl)-N-methylmethanesulfonamide
• 英文别名: N-[4-(4-fluorophenyl)-5-[(Z)-2-[(2S,4R)-4-hydroxy-6-oxooxan-2-yl]ethenyl]-6-propan-2-ylpyrimidin-2-yl]-N-methylmethanesulfonamide
• CAS: 1444772-05-7
• 化学式: C₂₂H₂₆FN₃O₅S
• 分子量: 463.53
• InChiKey: SOEGVMSNJOCVHT-CZDHMLMNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  32
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.41
• 拓扑面积：
  118
• 氢给体数：
  1
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  N-(4-(4-fluorophenyl)-5-((Z)-2-((2S,4R)-4-hydroxy-6-oxotetrahydro-2H-pyran-2-yl)vinyl)-6-isopropylpyrimidin-2-yl)-N-methylmethanesulfonamide 在 calcium chloride 、 sodium hydroxide 作用下， 以 四氢呋喃 、 水 为溶剂， 反应 20.0h， 以64%的产率得到(3R,5S,Z)-7-(4-(4-fluorophenyl)-6-isopropyl-2-(N-methylmethylsulfonamido)pyrimidin-5-yl)-3,5-dihydroxyhept-6-enoate calcium
  参考文献：
  名称：

  Conformational analysis of E/Z-isomeric pairs of rosuvastatin and its lactonized analogues

  摘要：

  Most of the super-statins contain a C=C double bond spacer between the heterocyclic and the chiral dihydroxycarboxylic moieties. The known drugs are E-geometric isomers, whereas very little is known about their Z-isomeric analogues. This study explains the unusual resonance line broadening observed in 1H NMR spectra of Z-isomeric rosuvastatin analogues at room temperature, which originates from dynamic exchange between different conformers. Conformational equilibria and intrinsic preferences of Z-isomeric rosuvastatin analogues provide valuable insight into conformational variability that is important for studying potential interactions within the binding site of the enzyme. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2013.05.020
• 作为产物：
  描述：

  N-(5-((Z)-2-((2S,4R)-4-(tert-butyldimethylsilyloxy)-6-oxotetrahydro-2H-pyran-2-yl)vinyl)-4-(4-fluorophenyl)-6-isopropylpyrimidin-2-yl)-N-methylmethanesulfonamide 在 溶剂黄146 、 tetra-n-butylammoniumfluoride trihydrate 作用下， 以 四氢呋喃 为溶剂， 反应 22.0h， 以55%的产率得到N-(4-(4-fluorophenyl)-5-((Z)-2-((2S,4R)-4-hydroxy-6-oxotetrahydro-2H-pyran-2-yl)vinyl)-6-isopropylpyrimidin-2-yl)-N-methylmethanesulfonamide
  参考文献：
  名称：

  Conformational analysis of E/Z-isomeric pairs of rosuvastatin and its lactonized analogues

  摘要：

  Most of the super-statins contain a C=C double bond spacer between the heterocyclic and the chiral dihydroxycarboxylic moieties. The known drugs are E-geometric isomers, whereas very little is known about their Z-isomeric analogues. This study explains the unusual resonance line broadening observed in 1H NMR spectra of Z-isomeric rosuvastatin analogues at room temperature, which originates from dynamic exchange between different conformers. Conformational equilibria and intrinsic preferences of Z-isomeric rosuvastatin analogues provide valuable insight into conformational variability that is important for studying potential interactions within the binding site of the enzyme. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2013.05.020

文献信息

• Conformational analysis of E/Z-isomeric pairs of rosuvastatin and its lactonized analogues
  作者：Jan Fabris、Damjan Makuc、Zdenko Časar、Janez Plavec

  DOI：10.1016/j.tet.2013.05.020

  日期：2013.7

  Most of the super-statins contain a C=C double bond spacer between the heterocyclic and the chiral dihydroxycarboxylic moieties. The known drugs are E-geometric isomers, whereas very little is known about their Z-isomeric analogues. This study explains the unusual resonance line broadening observed in 1H NMR spectra of Z-isomeric rosuvastatin analogues at room temperature, which originates from dynamic exchange between different conformers. Conformational equilibria and intrinsic preferences of Z-isomeric rosuvastatin analogues provide valuable insight into conformational variability that is important for studying potential interactions within the binding site of the enzyme. (C) 2013 Elsevier Ltd. All rights reserved.