6-(tert-butyl-dimethyl-silanyloxy)-5,5-dimethyl-2-phenylselanyl-hexanoic acid methyl ester | 916045-34-6

• 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: 6-(tert-butyl-dimethyl-silanyloxy)-5,5-dimethyl-2-phenylselanyl-hexanoic acid methyl ester
• CAS: 916045-34-6
• 化学式: C₂₁H₃₆O₃SeSi
• 分子量: 443.561
• InChiKey: ULBANDRTXGAZSL-UHFFFAOYSA-N

物化性质

• 沸点：
  448.4±45.0 °C(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.81
• 重原子数：
  26.0
• 可旋转键数：
  9.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  35.53
• 氢给体数：
  0.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  6-(tert-butyl-dimethyl-silanyloxy)-5,5-dimethyl-2-phenylselanyl-hexanoic acid methyl ester 在 sodium methylate 、 二异丁基氢化铝 、 三乙胺 、 lithium diisopropyl amide 作用下， 以 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：

  苯基氯化硒 、 Methyl 6-tert-butyldimethylsilyloxy-5,5-dimethylhexanoate 在 lithium diisopropyl amide 作用下， 以 四氢呋喃 为溶剂， 以77%的产率得到6-(tert-butyl-dimethyl-silanyloxy)-5,5-dimethyl-2-phenylselanyl-hexanoic acid methyl ester
  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