(2S,3R)-2-(benzyloxy)-3-(6-aminopurin-9-yl)-8,9-epoxynonane | 194783-27-2

• 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: (2S,3R)-2-(benzyloxy)-3-(6-aminopurin-9-yl)-8,9-epoxynonane
• 英文别名: 6-chloro-9-[(2S,3R)-7-(oxiran-2-yl)-2-phenylmethoxyheptan-3-yl]purine
• CAS: 194783-27-2
• 化学式: C₂₁H₂₅ClN₄O₂
• 分子量: 400.908
• InChiKey: RRROZHRPKVTZPR-DKKDMOBXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  28
• 可旋转键数：
  10
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.48
• 拓扑面积：
  65.4
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (2S,3R)-2-(benzyloxy)-3-(6-aminopurin-9-yl)-8,9-epoxynonane 在 高氯酸 作用下， 以 乙腈 为溶剂， 反应 2.0h， 以95%的产率得到(2S,3R)-2-(benzyloxy)-3-(6-chloropurin-9-yl)nonane-8,9-diol
  参考文献：
  名称：

  Adenosine Deaminase Inhibitors. Synthesis and Biological Evaluation of Putative Metabolites of (+)-erythro-9-(2S-Hydroxy-3R-nonyl)adenine

  摘要：

  The synthesis and biological evaluation of three chain-hydroxylated (+)-erythro-9-(2S-hydroxy-3R-nonyl)adenine [(+)-EHNA] derivatives are reported. Hydroxy groups at positions 9', 8', and 8',9' (12, 25, and 16) were introduced by either epoxidation or hydroboration of a terminal olefinic intermediate. Affinities for calf intestinal adenosine deaminase (ADA) were determined from the steady-state inhibition of adenosine deamination. K-i values of 0.82, 3.8, 6.4, and 15.8 nM were estimated for (+)-EHNA, 9'-hydroxy-(+)-EHNA (12), 8'-hydroxy-(+)-EHNA (25), and 8',9'-dihydroxy-(+)-EHNA (16), respectively, by assuming a single class of binding sites. However, the data for all inhibitors conformed more closely to the kinetics of a heterogeneous system with different affinities for two or more binding sites. The fairly high potencies of 12 and 25 suggest that other substitutions at the terminal position of the nonyl chain could yield useful ADA inhibitors.

  DOI：

  10.1021/jm00048a020
• 作为产物：
  描述：

  (2S,3S)-3-benzyloxy-1,2-epoxybutane 在 吡啶 、 盐酸 、 lithium aluminium tetrahydride 、 sodium azide 、 dilithium tetrachlorocuprate 、 三正丁胺 、 间氯过氧苯甲酸 作用下， 以 乙醚 、 二氯甲烷 、 戊醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 87.75h， 生成 (2S,3R)-2-(benzyloxy)-3-(6-aminopurin-9-yl)-8,9-epoxynonane
  参考文献：
  名称：

  Adenosine Deaminase Inhibitors. Synthesis and Biological Evaluation of Putative Metabolites of (+)-erythro-9-(2S-Hydroxy-3R-nonyl)adenine

  摘要：

  The synthesis and biological evaluation of three chain-hydroxylated (+)-erythro-9-(2S-hydroxy-3R-nonyl)adenine [(+)-EHNA] derivatives are reported. Hydroxy groups at positions 9', 8', and 8',9' (12, 25, and 16) were introduced by either epoxidation or hydroboration of a terminal olefinic intermediate. Affinities for calf intestinal adenosine deaminase (ADA) were determined from the steady-state inhibition of adenosine deamination. K-i values of 0.82, 3.8, 6.4, and 15.8 nM were estimated for (+)-EHNA, 9'-hydroxy-(+)-EHNA (12), 8'-hydroxy-(+)-EHNA (25), and 8',9'-dihydroxy-(+)-EHNA (16), respectively, by assuming a single class of binding sites. However, the data for all inhibitors conformed more closely to the kinetics of a heterogeneous system with different affinities for two or more binding sites. The fairly high potencies of 12 and 25 suggest that other substitutions at the terminal position of the nonyl chain could yield useful ADA inhibitors.

  DOI：

  10.1021/jm00048a020

文献信息

• Adenosine Deaminase Inhibitors. Synthesis and Biological Evaluation of Putative Metabolites of (+)-erythro-9-(2S-Hydroxy-3R-nonyl)adenine
  作者：Chandra Vargeese、Mallela S. P. Sarma、Palle V. P. Pragnacharyulu、Elie Abushanab、Shih-Ying Li、Johanna D. Stoeckler

  DOI：10.1021/jm00048a020

  日期：1994.10

  The synthesis and biological evaluation of three chain-hydroxylated (+)-erythro-9-(2S-hydroxy-3R-nonyl)adenine [(+)-EHNA] derivatives are reported. Hydroxy groups at positions 9', 8', and 8',9' (12, 25, and 16) were introduced by either epoxidation or hydroboration of a terminal olefinic intermediate. Affinities for calf intestinal adenosine deaminase (ADA) were determined from the steady-state inhibition of adenosine deamination. K-i values of 0.82, 3.8, 6.4, and 15.8 nM were estimated for (+)-EHNA, 9'-hydroxy-(+)-EHNA (12), 8'-hydroxy-(+)-EHNA (25), and 8',9'-dihydroxy-(+)-EHNA (16), respectively, by assuming a single class of binding sites. However, the data for all inhibitors conformed more closely to the kinetics of a heterogeneous system with different affinities for two or more binding sites. The fairly high potencies of 12 and 25 suggest that other substitutions at the terminal position of the nonyl chain could yield useful ADA inhibitors.