Methyl 6-tert-butyldimethylsilyloxy-5,5-dimethylhexanoate | 290812-14-5

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: Methyl 6-tert-butyldimethylsilyloxy-5,5-dimethylhexanoate
• 英文别名: Methyl 6-[tert-butyl(dimethyl)silyl]oxy-5,5-dimethylhexanoate
• CAS: 290812-14-5
• 化学式: C₁₅H₃₂O₃Si
• 分子量: 288.503
• InChiKey: XVDXYHDCEHBWJJ-UHFFFAOYSA-N

物化性质

• 沸点：
  299.8±23.0 °C(Predicted)
• 密度：
  0.896±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.38
• 重原子数：
  19
• 可旋转键数：
  9
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.93
• 拓扑面积：
  35.5
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  Methyl 6-tert-butyldimethylsilyloxy-5,5-dimethylhexanoate 在 sodium methylate 、 二异丁基氢化铝 、 三乙胺 、 lithium diisopropyl amide 作用下， 以 四氢呋喃 、 甲醇 、 甲苯 为溶剂， 生成 tert-butyl-dimethyl-[(7E)-2,2,8,12-tetramethyl-5-methylidenetrideca-7,11-dienoxy]silane
  参考文献：
  名称：

  Degradation and Reconstruction of Moenomycin A and Derivatives:  Dissecting the Function of the Isoprenoid Chain

  摘要：

  Moenomycin A is the only known natural product that inhibits peptidoglycan biosynthesis by binding the bacterial transglycosylases. We describe a degradation/reconstruction route to manipulate the reducing end of moenomycin A. A comparison of the biological and enzyme inhibitory activity of moenomycin A and an analogue containing a nerol lipid in place of the natural C25 lipid chain provides insight into the role of the moenocinol unit. Our results show that a lipid chain having ten carbons in moenocinol is sufficient for enzyme inhibition, but a longer chain is required for biological acitivity, apparently because the molecule must partition into biological membranes to reach its target in bacterial cells.

  DOI：

  10.1021/ja065905c
• 作为产物：
  描述：

  4-tert-butyldimethylsilyloxy-3,3-dimethylbutanal 在 magnesium 作用下， 以 苯 为溶剂， 反应 52.0h， 生成 Methyl 6-tert-butyldimethylsilyloxy-5,5-dimethylhexanoate
  参考文献：
  名称：

  信息素合成，CCVIII：(1S,3S,7R)-3-Methyl-α-himachalene 的合成，巴西 Jacobina 长须白蛉的性信息素

  摘要：

  (通过采用 Evan 或 Oppolzer 的不对称甲基化和分子内 Diels-Alder 反应这两个关键步骤，对映体选择性地合成了 (1S,3S,7R)-3-甲基-δ-himachalene，它是巴西雅各比纳雄性沙蝇（Lutzomyia longipalpis）的性信息素。通过对与合成中间体之一相关的化合物进行 X 射线分析，明确确定了产物的绝对构型。这种沙蝇信息素的环结具有与已知植物来源的(1R,7R)-δ-himachalene相反的绝对构型。

  DOI：

  10.1055/s-2000-8220

文献信息

• [EN] MOENOMYCIN ANALOGS, METHODS OF SYNTHESIS, AND USES THEREOF<br/>[FR] ANALOGUES DE LA MOÉNOMYCINE, PROCÉDÉS DE SYNTHÈSE ET UTILISATIONS DE CEUX-CI
  申请人：HARVARD COLLEGE

  公开号：WO2009046314A3

  公开（公告）日：2009-05-22
• Pheromone Synthesis, CCVIII: Synthesis of (1S,3S,7R)-3-Methyl-α-himachalene, the Sex Pheromone of the Sandfly Lutzomyia longipalpis from Jacobina, Brazil
  作者：Takuya Tashiro、Masahiko Bando、Kenji Mori

  DOI：10.1055/s-2000-8220

  日期：——

  (1S,3S,7R)-3-Methyl-α-himachalene, the sex pheromone of the male sandfly (Lutzomyia longipalpis) from Jacobina, Brazil, was synthesized enantioselectively by employing Evan's or Oppolzer's asymmetric methylation and intramolecular Diels-Alder reaction as the two key steps. The absolute configuration of the product was unambiguously established by X-ray analysis of a compound related to one of the synthetic intermediates. The ring junction of this sandfly pheromone possesses the absolute configuration opposite to that of the known (1R,7R)-α-himachalene of plant origin.

  (通过采用 Evan 或 Oppolzer 的不对称甲基化和分子内 Diels-Alder 反应这两个关键步骤，对映体选择性地合成了 (1S,3S,7R)-3-甲基-δ-himachalene，它是巴西雅各比纳雄性沙蝇（Lutzomyia longipalpis）的性信息素。通过对与合成中间体之一相关的化合物进行 X 射线分析，明确确定了产物的绝对构型。这种沙蝇信息素的环结具有与已知植物来源的(1R,7R)-δ-himachalene相反的绝对构型。
• Degradation and Reconstruction of Moenomycin A and Derivatives:  Dissecting the Function of the Isoprenoid Chain
  作者：Masaatsu Adachi、Yi Zhang、Catherine Leimkuhler、Binyuan Sun、John V. LaTour、Daniel E. Kahne

  DOI：10.1021/ja065905c

  日期：2006.11.1

  Moenomycin A is the only known natural product that inhibits peptidoglycan biosynthesis by binding the bacterial transglycosylases. We describe a degradation/reconstruction route to manipulate the reducing end of moenomycin A. A comparison of the biological and enzyme inhibitory activity of moenomycin A and an analogue containing a nerol lipid in place of the natural C25 lipid chain provides insight into the role of the moenocinol unit. Our results show that a lipid chain having ten carbons in moenocinol is sufficient for enzyme inhibition, but a longer chain is required for biological acitivity, apparently because the molecule must partition into biological membranes to reach its target in bacterial cells.