diphosphoryl-(2'R,5'R)-9-(5-phosphonylmethoxy-2,5-dihydrofuran-2-yl)adenine

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 咪唑并嘧啶类
• 英文名称: diphosphoryl-(2'R,5'R)-9-(5-phosphonylmethoxy-2,5-dihydrofuran-2-yl)adenine
• 英文别名: 9-[5-({[(Phosphonooxy)(hydroxyphosphoryl)oxy](hydroxyphosphoryl)}methoxy)-2-2,5-dihydrofuryl]purine-6-ylamine；[(2R,5R)-5-(6-aminopurin-9-yl)-2,5-dihydrofuran-2-yl]oxymethyl-[hydroxy(phosphonooxy)phosphoryl]oxyphosphinic acid
• 化学式: C₁₀H₁₄N₅O₁₁P₃
• 分子量: 473.169
• InChiKey: SQEYXKDKELYPOZ-RQJHMYQMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.6
• 重原子数：
  29
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  239
• 氢给体数：
  5
• 氢受体数：
  15

反应信息

• 作为产物：
  描述：

  (2R,5R)-9-<2,5-dihydro-5-(phosphonomethoxy)-2-furanyl>adenine ammonium salt 在 N,N'-羰基二咪唑 、 三丁基焦磷酸铵 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 6.0h， 以40%的产率得到diphosphoryl-(2'R,5'R)-9-(5-phosphonylmethoxy-2,5-dihydrofuran-2-yl)adenine
  参考文献：
  名称：

  Isosteric triphosphonate analogues of dNTP: Synthesis and substrate properties toward various DNA polymerases

  摘要：

  Isosteric triphosphonate derivatives of 2',3'-dideoxy-2',3'-didehydroadenosine and 3'-deoxy-2',3'-didehydrothymidine and their beta,gamma-substituted analogues were synthesized. Their substrate properties toward a number of reverse transcriptases of the human immunodeficiency and avian myeloblastosis viruses, human DNA polymerases alpha and beta, and the Klenow fragment of Escherichia coli DNA polymerase I were studied.

  DOI：

  10.1134/s1068162007050056

文献信息

• Isosteric triphosphonate analogues of dNTP: Synthesis and substrate properties toward various DNA polymerases
  作者：A. Yu. Skoblov、A. N. Semenyuk、A. M. Murabuldaev、V. V. Sosunov、L. S. Viktorova、Yu. S. Skoblov

  DOI：10.1134/s1068162007050056

  日期：2007.9

  Isosteric triphosphonate derivatives of 2',3'-dideoxy-2',3'-didehydroadenosine and 3'-deoxy-2',3'-didehydrothymidine and their beta,gamma-substituted analogues were synthesized. Their substrate properties toward a number of reverse transcriptases of the human immunodeficiency and avian myeloblastosis viruses, human DNA polymerases alpha and beta, and the Klenow fragment of Escherichia coli DNA polymerase I were studied.