Phosphoric acid (R)-2-acetylamino-9-hydroxy-nonyl ester methyl ester | 223681-47-8

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• 英文名称: Phosphoric acid (R)-2-acetylamino-9-hydroxy-nonyl ester methyl ester
• 英文别名: [(2R)-2-acetamido-9-hydroxynonyl] methyl hydrogen phosphate
• CAS: 223681-47-8
• 化学式: C₁₂H₂₆NO₆P
• 分子量: 311.315
• InChiKey: HCDXERBXMHCKMI-GFCCVEGCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.2
• 重原子数：
  20
• 可旋转键数：
  12
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  105
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  cholesteryl hemisuccinoyl chloride 、 Phosphoric acid (R)-2-acetylamino-9-hydroxy-nonyl ester methyl ester 在 4-二甲氨基吡啶 、 三乙胺 作用下， 以 氯仿 为溶剂， 生成 Succinic acid (R)-8-acetylamino-9-(hydroxy-methoxy-phosphoryloxy)-nonyl ester (3S,8S,9S,10R,13R,14S,17R)-17-((R)-1,5-dimethyl-hexyl)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-3-yl ester
  参考文献：
  名称：

  Synthesis and PLA2-inhibitory properties of 2(R)-acetamido-alkylphosphomethanols with a variable aggregate anchor

  摘要：

  Acylamino inhibitors of 14 kDa-PLA(2) were synthesized which differ in the moiety that is not bound into the enzyme's active site but immersed in the lipid aggregate when a ternary inhibitory complex is formed. Our results indicate that this part of the inhibitors does not significantly influence inhibitory properties as long the amphiphilic character is retained. So, inhibitory and biophysical properties should be variable independently. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(98)00721-5
• 作为产物：
  描述：

  (R)-4-((E)-7-Benzyloxy-hept-1-enyl)-2-methoxy-[1,3,2]oxazaphospholidine 2-oxide 在 palladium on activated charcoal 盐酸 、 4-二甲氨基吡啶 、 甲酸 、 氢气 、 三乙胺 作用下， 以 甲醇 、 氯仿 、 甲苯 为溶剂， 生成 Phosphoric acid (R)-2-acetylamino-9-hydroxy-nonyl ester methyl ester
  参考文献：
  名称：

  Synthesis and PLA2-inhibitory properties of 2(R)-acetamido-alkylphosphomethanols with a variable aggregate anchor

  摘要：

  Acylamino inhibitors of 14 kDa-PLA(2) were synthesized which differ in the moiety that is not bound into the enzyme's active site but immersed in the lipid aggregate when a ternary inhibitory complex is formed. Our results indicate that this part of the inhibitors does not significantly influence inhibitory properties as long the amphiphilic character is retained. So, inhibitory and biophysical properties should be variable independently. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(98)00721-5