9-[(3aR,4R,6R,6aR)-2,2-dimethyl-6-(pyridin-3-ylmethoxymethyl)-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-4-yl]-8-N-methylpurine-6,8-diamine | 1309803-42-6

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷
• 英文名称: 9-[(3aR,4R,6R,6aR)-2,2-dimethyl-6-(pyridin-3-ylmethoxymethyl)-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-4-yl]-8-N-methylpurine-6,8-diamine
• CAS: 1309803-42-6
• 化学式: C₂₀H₂₅N₇O₄
• 分子量: 427.463
• InChiKey: JAAXWLFWOWQUAI-SCFUHWHPSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.4
• 重原子数：
  31
• 可旋转键数：
  6
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  132
• 氢给体数：
  2
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  8-bromo-2',3'-O-isopropylene adenosine 在 caesium carbonate 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.75h， 生成 9-[(3aR,4R,6R,6aR)-2,2-dimethyl-6-(pyridin-3-ylmethoxymethyl)-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-4-yl]-8-N-methylpurine-6,8-diamine 、 [(3aR,4R,6R,6aR)-4-[6-amino-8-[methyl(pyridin-3-ylmethyl)amino]purin-9-yl]-2,2-dimethyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-6-yl]methanol
  参考文献：
  名称：

  Adenosine-Derived Inhibitors of 78 kDa Glucose Regulated Protein (Grp78) ATPase: Insights into Isoform Selectivity

  摘要：

  78 kDa glucose-regulated protein (Grp78) is a heat shock protein (HSP) involved in protein folding that plays a role in cancer cell proliferation. Binding of adenosine-derived inhibitors to Grp78 was characterized by surface plasmon resonance and isothermal titration calorimetry. The most potent compounds were 13 (VER-155008) with K-D = 80 nM and 14 with K-D = 60 nM. X-ray crystal structures of Grp78 bound to ATP, ADPnP, and adenosine derivative 10 revealed differences in the binding site between Grp78 and homologous proteins.

  DOI：

  10.1021/jm101625x

文献信息

• Adenosine-Derived Inhibitors of 78 kDa Glucose Regulated Protein (Grp78) ATPase: Insights into Isoform Selectivity
  作者：Alba T. Macias、Douglas S. Williamson、Nicola Allen、Jenifer Borgognoni、Alexandra Clay、Zoe Daniels、Pawel Dokurno、Martin J. Drysdale、Geraint L. Francis、Christopher J. Graham、Rob Howes、Natalia Matassova、James B. Murray、Rachel Parsons、Terry Shaw、Allan E. Surgenor、Lindsey Terry、Yikang Wang、Mike Wood、Andrew J. Massey

  DOI：10.1021/jm101625x

  日期：2011.6.23

  78 kDa glucose-regulated protein (Grp78) is a heat shock protein (HSP) involved in protein folding that plays a role in cancer cell proliferation. Binding of adenosine-derived inhibitors to Grp78 was characterized by surface plasmon resonance and isothermal titration calorimetry. The most potent compounds were 13 (VER-155008) with K-D = 80 nM and 14 with K-D = 60 nM. X-ray crystal structures of Grp78 bound to ATP, ADPnP, and adenosine derivative 10 revealed differences in the binding site between Grp78 and homologous proteins.