2,6-naphthalenedicarbonyl bis(dimethyl phosphate)

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 2,6-naphthalenedicarbonyl bis(dimethyl phosphate)
• 英文别名: Bis(dimethoxyphosphoryl) naphthalene-2,6-dicarboxylate
• 化学式: C₁₆H₁₈O₁₀P₂
• 分子量: 432.26
• InChiKey: FGHSIOAWUSHHQX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.8
• 重原子数：
  28
• 可旋转键数：
  10
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  124
• 氢给体数：
  0
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  2,6-naphthalenedicarbonyl bis(dimethyl phosphate) 在 sodium iodide 作用下， 以 乙腈 为溶剂， 反应 12.0h， 以96%的产率得到Bis[hydroxy(methoxy)phosphoryl] naphthalene-2,6-dicarboxylate
  参考文献：
  名称：

  Systematically Cross-Linked Human Hemoglobin:  Functional Effects of 10 Å Spans between Beta Subunits at Lysine-82

  摘要：

  The structure and properties of hemoglobin are altered by the introduction of cross-links of defined structure between specific residues, The bis methyl phosphates and bis 3,5-dibromosalicylates of 4-carbuxy-trans-cinnamic acid as well as the bis methyl phosphate of 2,6-naphthalenedicarboxylic acid produce a 10 Angstrom cross-link between the epsilon-amino groups of each beta-lys-82 of human hemoglobin. The oxygen affinity of the modified proteins fits the correlation interpolated from those for shorter and longer cross-links. The oxygen binding curve shows a high degree of cooperativity. These results support the idea that the length of the semirigid cross-link in a structurally homogeneous series constrains the relaxation of the protein upon oxygen binding by a mechanism that is specifically reflected in the oxygen affinity, while interactions between hemes that affect cooperativity are not diminished.

  DOI：

  10.1021/ja961443z
• 作为产物：
  描述：

  2,6-萘二羧酸 在 草酰氯 、 N,N-二甲基甲酰胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 7.0h， 生成 2,6-naphthalenedicarbonyl bis(dimethyl phosphate)
  参考文献：
  名称：

  Systematically Cross-Linked Human Hemoglobin:  Functional Effects of 10 Å Spans between Beta Subunits at Lysine-82

  摘要：

  The structure and properties of hemoglobin are altered by the introduction of cross-links of defined structure between specific residues, The bis methyl phosphates and bis 3,5-dibromosalicylates of 4-carbuxy-trans-cinnamic acid as well as the bis methyl phosphate of 2,6-naphthalenedicarboxylic acid produce a 10 Angstrom cross-link between the epsilon-amino groups of each beta-lys-82 of human hemoglobin. The oxygen affinity of the modified proteins fits the correlation interpolated from those for shorter and longer cross-links. The oxygen binding curve shows a high degree of cooperativity. These results support the idea that the length of the semirigid cross-link in a structurally homogeneous series constrains the relaxation of the protein upon oxygen binding by a mechanism that is specifically reflected in the oxygen affinity, while interactions between hemes that affect cooperativity are not diminished.

  DOI：

  10.1021/ja961443z