pentanedioic acid 5-carboxypentyl ester hexyl ester | 915778-45-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: pentanedioic acid 5-carboxypentyl ester hexyl ester
• 英文别名: 6-{[5-(Hexyloxy)-5-oxopentanoyl]oxy}hexanoic acid；6-(5-hexoxy-5-oxopentanoyl)oxyhexanoic acid
• CAS: 915778-45-9
• 化学式: C₁₇H₃₀O₆
• 分子量: 330.422
• InChiKey: PIXIXGCJTAARAF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  23
• 可旋转键数：
  17
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.82
• 拓扑面积：
  89.9
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  pentanedioic acid 5-carboxypentyl ester hexyl ester 、 三甲基乙酰氯 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 24.0h， 生成
  参考文献：
  名称：

  Sodium Ion Internalized within Phospholipid Membranes

  摘要：

  Seven phospholipids, modified with ester groups in their hydrophobic chains, were synthesized and examined for their ability to promote sodium ion flux across vesicular membranes. It was found by 23Na NMR that only the phospholipids having short chain segments beyond their terminal ester groups catalyze sodium ion transfer by up to 2 orders of magnitude relative to a conventional phospholipid, POPC. The rates increase with the concentration of the ester-phospholipid admixed with POPC in the bilayer. More surprisingly, the rates increase with the time allowed for the vesicles to age. This was attributed to ester-phospholipid migrating in the bilayers to form domains that solubilize the sodium ion within the hydrocarbon interior of the membrane. Such membrane domains explain why shift reagent-modified NMR spectra display three 23Na signals representing sodium outside the vesicles, sodium within the vesicular water pools, and sodium within the membranes themselves.

  DOI：

  10.1021/ja065702o
• 作为产物：
  描述：

  戊二酸单己基酯 在 吡啶 、 2,2,6,6-tetramethyl-piperidine-N-oxyl 、 氯化亚砜 、 三氯异氰尿酸 、 sodium bromide 作用下， 以 氯仿 、 碳酸氢钠 、 丙酮 为溶剂， 反应 24.0h， 生成 pentanedioic acid 5-carboxypentyl ester hexyl ester
  参考文献：
  名称：

  Sodium Ion Internalized within Phospholipid Membranes

  摘要：

  Seven phospholipids, modified with ester groups in their hydrophobic chains, were synthesized and examined for their ability to promote sodium ion flux across vesicular membranes. It was found by 23Na NMR that only the phospholipids having short chain segments beyond their terminal ester groups catalyze sodium ion transfer by up to 2 orders of magnitude relative to a conventional phospholipid, POPC. The rates increase with the concentration of the ester-phospholipid admixed with POPC in the bilayer. More surprisingly, the rates increase with the time allowed for the vesicles to age. This was attributed to ester-phospholipid migrating in the bilayers to form domains that solubilize the sodium ion within the hydrocarbon interior of the membrane. Such membrane domains explain why shift reagent-modified NMR spectra display three 23Na signals representing sodium outside the vesicles, sodium within the vesicular water pools, and sodium within the membranes themselves.

  DOI：

  10.1021/ja065702o

文献信息

• Sodium Ion Internalized within Phospholipid Membranes
  作者：Fredric M. Menger、Ashley L. Galloway、Mary E. Chlebowski、Shaoxing Wu

  DOI：10.1021/ja065702o

  日期：2006.11.1

  Seven phospholipids, modified with ester groups in their hydrophobic chains, were synthesized and examined for their ability to promote sodium ion flux across vesicular membranes. It was found by 23Na NMR that only the phospholipids having short chain segments beyond their terminal ester groups catalyze sodium ion transfer by up to 2 orders of magnitude relative to a conventional phospholipid, POPC. The rates increase with the concentration of the ester-phospholipid admixed with POPC in the bilayer. More surprisingly, the rates increase with the time allowed for the vesicles to age. This was attributed to ester-phospholipid migrating in the bilayers to form domains that solubilize the sodium ion within the hydrocarbon interior of the membrane. Such membrane domains explain why shift reagent-modified NMR spectra display three 23Na signals representing sodium outside the vesicles, sodium within the vesicular water pools, and sodium within the membranes themselves.