1,2-二棕榈酰基-sn-甘油-3-磷酸乙醇胺-N-[3-(2-吡啶基二硫代)丙酸酯](钠盐) | 474944-16-6

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 甘油磷脂
• 中文名称: 1,2-二棕榈酰基-sn-甘油-3-磷酸乙醇胺-N-[3-(2-吡啶基二硫代)丙酸酯](钠盐)
• 英文名称: N-(3-(2-pyridinyldithio)propionyl)dipalmitoyl phosphatidylethanolamine sodium salt
• 英文别名: sodium;N-[2-[[(2R)-2,3-di(hexadecanoyloxy)propoxy]-hydroxyphosphoryl]oxyethyl]-3-(pyridin-2-yldisulfanyl)propanimidate
• CAS: 474944-16-6
• 化学式: C₄₅H₈₀N₂O₉PS₂*Na
• 分子量: 911.234
• InChiKey: IUSHQKJFHVODPF-QUEDAWNRSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  9.25
• 重原子数：
  60
• 可旋转键数：
  45
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.82
• 拓扑面积：
  204
• 氢给体数：
  1
• 氢受体数：
  12

反应信息

• 作为反应物：
  描述：

  1,2-二棕榈酰基-sn-甘油-3-磷酸乙醇胺-N-[3-(2-吡啶基二硫代)丙酸酯](钠盐) 、 以 甲醇 、 氯仿 为溶剂， 反应 48.0h， 以54 mg的产率得到(myristoyl)glycyl-S-(hexadecyl)cysteinyl-4,5-dithia-7-aminoheptanoyl-dipalmitoyl phosphatidylethanolamine, sodium salt
  参考文献：
  名称：

  Sorting of Lipidated Peptides in Fluid Bilayers: A Molecular-Level Investigation

  摘要：

  Nearest-neighbor recognition (NNR) measurements have been made for two lipidated forms of GlyCys, interacting with analogues of cholesterol and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) in the liquid-ordered (l(o)) and liquid-disordered (l(d)) phases. Interaction free energies that have been determined from these measurements have been used in Monte Carlo simulations to quantify the distribution of the peptides between liquid-ordered and liquid-disordered regions. These simulations have shown that significant differences in the lipid chains have a very weak influence on the partitioning of the peptide between these two phases. They have also revealed an insensitivity of the peptide partition coefficient, K-p, to the size of the l(o) and l(d) domains that are present. In a broader context, these findings strongly suggest that the sorting of peripheral proteins in cellular membranes via differential lipidation may be more subtle than previously thought.

  DOI：

  10.1021/ja3074825
• 作为产物：
  描述：

  L-磷脂酰乙醇胺 、 N--3-(2-pyridyldithio)propionate 在 N,N-二异丙基乙胺 作用下， 以 甲醇 、 氯仿 、 水 为溶剂， 反应 4.0h， 以85%的产率得到1,2-二棕榈酰基-sn-甘油-3-磷酸乙醇胺-N-[3-(2-吡啶基二硫代)丙酸酯](钠盐)
  参考文献：
  名称：

  Sorting of Lipidated Peptides in Fluid Bilayers: A Molecular-Level Investigation

  摘要：

  Nearest-neighbor recognition (NNR) measurements have been made for two lipidated forms of GlyCys, interacting with analogues of cholesterol and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) in the liquid-ordered (l(o)) and liquid-disordered (l(d)) phases. Interaction free energies that have been determined from these measurements have been used in Monte Carlo simulations to quantify the distribution of the peptides between liquid-ordered and liquid-disordered regions. These simulations have shown that significant differences in the lipid chains have a very weak influence on the partitioning of the peptide between these two phases. They have also revealed an insensitivity of the peptide partition coefficient, K-p, to the size of the l(o) and l(d) domains that are present. In a broader context, these findings strongly suggest that the sorting of peripheral proteins in cellular membranes via differential lipidation may be more subtle than previously thought.

  DOI：

  10.1021/ja3074825

文献信息

• Sorting of Lipidated Peptides in Fluid Bilayers: A Molecular-Level Investigation
  作者：Trevor A. Daly、Paulo F. Almeida、Steven L. Regen

  DOI：10.1021/ja3074825

  日期：2012.10.17

  Nearest-neighbor recognition (NNR) measurements have been made for two lipidated forms of GlyCys, interacting with analogues of cholesterol and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) in the liquid-ordered (l(o)) and liquid-disordered (l(d)) phases. Interaction free energies that have been determined from these measurements have been used in Monte Carlo simulations to quantify the distribution of the peptides between liquid-ordered and liquid-disordered regions. These simulations have shown that significant differences in the lipid chains have a very weak influence on the partitioning of the peptide between these two phases. They have also revealed an insensitivity of the peptide partition coefficient, K-p, to the size of the l(o) and l(d) domains that are present. In a broader context, these findings strongly suggest that the sorting of peripheral proteins in cellular membranes via differential lipidation may be more subtle than previously thought.