N-acetyl-α-D-muramic acid, 1-O-(hexadecyl hydrogen phosphate) | 170873-72-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N-acetyl-α-D-muramic acid, 1-O-(hexadecyl hydrogen phosphate)
• 英文别名: (2R)-2-[(2R,3R,4R,5S,6R)-3-acetamido-2-[hexadecoxy(hydroxy)phosphoryl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxypropanoic acid
• CAS: 170873-72-0
• 化学式: C₂₇H₅₂NO₁₁P
• 分子量: 597.684
• InChiKey: XVQOPSJFVDMSEE-IDFMNTPUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.1
• 重原子数：
  40
• 可旋转键数：
  23
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.93
• 拓扑面积：
  181
• 氢给体数：
  5
• 氢受体数：
  11

反应信息

• 作为产物：
  描述：

  benzyl hexadecyl diisopropylphosphoramidite 在 四氮唑 、 palladium 10% on activated carbon 、 氢气 、 双氧水 、 lithium hydroxide 作用下， 以 甲醇 、 水 、 乙腈 为溶剂， -78.0~20.0 ℃ 、101.33 kPa 条件下， 反应 27.58h， 生成 N-acetyl-α-D-muramic acid, 1-O-(hexadecyl hydrogen phosphate)
  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

文献信息

• Synthesis of Modified Peptidoglycan Precursor Analogues for the Inhibition of Glycosyltransferase
  作者：Shrinivas Dumbre、Adeline Derouaux、Eveline Lescrinier、André Piette、Bernard Joris、Mohammed Terrak、Piet Herdewijn

  DOI：10.1021/ja302099u

  日期：2012.6.6

  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.