2-chloro-6-((3-iodobenzyl)amino)-9-cyclopentylpurine | 240820-01-3

• 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: 2-chloro-6-((3-iodobenzyl)amino)-9-cyclopentylpurine
• 英文别名: 2-chloro-9-cyclopentyl-N-[(3-iodophenyl)methyl]purin-6-amine
• CAS: 240820-01-3
• 化学式: C₁₇H₁₇ClIN₅
• 分子量: 453.713
• InChiKey: RMSOBUYTHXBZMT-UHFFFAOYSA-N

物化性质

• 沸点：
  565.2±60.0 °C(Predicted)
• 密度：
  1.82±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.6
• 重原子数：
  24
• 可旋转键数：
  4
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  55.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  1,4-环己烷二胺 、 2-chloro-6-((3-iodobenzyl)amino)-9-cyclopentylpurine 反应 18.0h， 以92%的产率得到2-[trans-(4-aminocyclohexyl)amino]-6-(3-iodobenzylamino)-9-cyclopentylpurine
  参考文献：
  名称：

  6,9-DISUBSTITUTED 2- TRANS-(4- AMINOCYCLOHEXYL) AMINO]PURINES

  摘要：

  公开号：

  EP1056745B1
• 作为产物：
  描述：

  环戊醇 在 N,N-二异丙基乙胺 、 三苯基膦 、 偶氮二甲酸二乙酯 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 48.0h， 生成 2-chloro-6-((3-iodobenzyl)amino)-9-cyclopentylpurine
  参考文献：
  名称：

  Crystal Structure of Human Cyclin-Dependent Kinase 2 in Complex with the Adenine-Derived Inhibitor H717

  摘要：

  Cyclin-dependent kinases (CDKs) are regulatory proteins of the eukaryotic cell cycle. They act after association with different cyclins, the concentrations of which vary throughout the progression of the cell cycle. As central mediators of cell growth, CDKs are potential targets for inhibitory molecules that would allow disruption of the cell cycle in order to evoke an antiproliferative effect and may therefore be useful as cancer therapeutics. We synthesized several inhibitory 2,6,9-trisubstituted purine derivatives and solved the crystal structure of one of these compounds, H717, in complex with human CDK2 at 2.6 Angstrom resolution. The orientation of the C-2-p-diaminocyclohexyl portion of the inhibitor is strikingly different from those of similar moieties in other related inhibitor complexes. The N-9-cyclopentyl ring fully occupies a space in the enzyme which is otherwise empty, while the C-6-N-aminobenzyl substituent points out of the ATP-binding site. The structure provides a basis for the further development of more potent inhibitory drugs.

  DOI：

  10.1021/jm001043t