(2R)-3-[[(2R,3R,4R,5S,6R)-3-acetamido-4-[(1R)-1-carboxyethoxy]-5-hydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-hydroxyphosphoryl]oxy-2-[(2E)-3,7-dimethylocta-2,6-dienoxy]propanoic acid | 1380522-34-8

• 分子结构分类: 有机化合物 - 脂质和类脂质分子
• 英文名称: (2R)-3-[[(2R,3R,4R,5S,6R)-3-acetamido-4-[(1R)-1-carboxyethoxy]-5-hydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-hydroxyphosphoryl]oxy-2-[(2E)-3,7-dimethylocta-2,6-dienoxy]propanoic acid
• CAS: 1380522-34-8
• 化学式: C₂₄H₄₀NO₁₄P
• 分子量: 597.554
• InChiKey: QNHDJXFVYGVKAP-HLGHKOFHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.2
• 重原子数：
  40
• 可旋转键数：
  17
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  228
• 氢给体数：
  6
• 氢受体数：
  14

反应信息

• 作为产物：
  描述：

  在 四丁基氟化铵 、 金刚烷酰氯 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 、 lithium hydroxide 作用下， 以 四氢呋喃 、 吡啶 、 二氯甲烷 、 水 为溶剂， 反应 22.0h， 生成 (2R)-3-[[(2R,3R,4R,5S,6R)-3-acetamido-4-[(1R)-1-carboxyethoxy]-5-hydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-hydroxyphosphoryl]oxy-2-[(2E)-3,7-dimethylocta-2,6-dienoxy]propanoic acid
  参考文献：
  名称：

  Synthesis of Modified Peptidoglycan Precursor Analogues for the Inhibition of Glycosyltransferase

  摘要：

  The peptidoglycan glycosyltransferases (GTs) are essential enzymes that catalyze the polymerization of On OH glycan chains of the bacterial cell wall from lipid II and thus constitute a validated antibacterial target. Their enzymatic cavity is composed of a donor site for the growing glycan chain (where the inhibitor moenomycin binds) and an acceptor site for lipid II substrate. In order to find lead inhibitors able to fill this large active site, we have synthesized a series of substrate analogues of lipid I and lipid II with variations in the lipid, the pyrophosphate, and the peptide moieties and evaluated their biological effect on the GT activity of E. coli PBP1b and their antibacterial potential. We found several compounds able to inhibit the GT activity in vitro and cause growth defect in Bacillus subtilis. The more active was C16-phosphoglycerate-MurNAc-(L-Alao-D-Glu)-GIcNAc, which also showed antibacterial activity. These molecules are promising leads for the design of new antibacterial GT inhibitors.

  DOI：

  10.1021/ja302099u