3,3'-<(2,6-pyrazinediyl 4-oxide)bis(oxy)>bis(benzonitrile) | 228393-50-8

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3,3'-<(2,6-pyrazinediyl 4-oxide)bis(oxy)>bis(benzonitrile)
• 英文别名: 3-[6-(3-Cyanophenoxy)-4-oxidopyrazin-4-ium-2-yl]oxybenzonitrile
• CAS: 228393-50-8
• 化学式: C₁₈H₁₀N₄O₃
• 分子量: 330.302
• InChiKey: IQMYOTWKOABODI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  25
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  104
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  3,3'-<(2,6-pyrazinediyl 4-oxide)bis(oxy)>bis(benzonitrile) 在 盐酸 、 氨 作用下， 以 乙醇 为溶剂， 反应 18.0h， 生成 3,3'-<(pyrazine-2,6-diyl 4-oxide)3is(oxy)>bis(benzenecarboximidamide)
  参考文献：
  名称：

  Design, Synthesis, and Activity of 2,6-Diphenoxypyridine-Derived Factor Xa Inhibitors

  摘要：

  A novel series of 2,6-diphenoxypyridines has been designed to inhibit factor Xa, a serine protease strategically located in the coagulation cascade. The evolution from the photochemically unstable bisamidine (Z,Z)-BABCH to potent bisamidine compounds with a pyridine heterocycle as the core scaffold has been achieved. The most potent compound in the series, 6h, has a K-i for human factor Xa of 12 nM. The selectivity of 6h against bovine trypsin and human thrombin was greater than 90- and 1000-fold, respectively. Two proposed modes of binding of 6h Do factor Xa are made based on the crystal structures of 6h by itself and of 6h bound to bovine trypsin.

  DOI：

  10.1021/jm980667k
• 作为产物：
  描述：

  3,3'-<2,6-pyrazinediylbis(oxy)>bis(benzonitrile) 在 双氧水 、 溶剂黄146 作用下， 反应 24.0h， 以35%的产率得到3,3'-<(2,6-pyrazinediyl 4-oxide)bis(oxy)>bis(benzonitrile)
  参考文献：
  名称：

  Design, Synthesis, and Activity of 2,6-Diphenoxypyridine-Derived Factor Xa Inhibitors

  摘要：

  A novel series of 2,6-diphenoxypyridines has been designed to inhibit factor Xa, a serine protease strategically located in the coagulation cascade. The evolution from the photochemically unstable bisamidine (Z,Z)-BABCH to potent bisamidine compounds with a pyridine heterocycle as the core scaffold has been achieved. The most potent compound in the series, 6h, has a K-i for human factor Xa of 12 nM. The selectivity of 6h against bovine trypsin and human thrombin was greater than 90- and 1000-fold, respectively. Two proposed modes of binding of 6h Do factor Xa are made based on the crystal structures of 6h by itself and of 6h bound to bovine trypsin.

  DOI：

  10.1021/jm980667k

文献信息

• Design, Synthesis, and Activity of 2,6-Diphenoxypyridine-Derived Factor Xa Inhibitors
  作者：Gary Phillips、David D. Davey、Keith A. Eagen、Sunil K. Koovakkat、Amy Liang、Howard P. Ng、Michael Pinkerton、Lan Trinh、Marc Whitlow、Alicia M. Beatty、Michael M. Morrissey

  DOI：10.1021/jm980667k

  日期：1999.5.1

  A novel series of 2,6-diphenoxypyridines has been designed to inhibit factor Xa, a serine protease strategically located in the coagulation cascade. The evolution from the photochemically unstable bisamidine (Z,Z)-BABCH to potent bisamidine compounds with a pyridine heterocycle as the core scaffold has been achieved. The most potent compound in the series, 6h, has a K-i for human factor Xa of 12 nM. The selectivity of 6h against bovine trypsin and human thrombin was greater than 90- and 1000-fold, respectively. Two proposed modes of binding of 6h Do factor Xa are made based on the crystal structures of 6h by itself and of 6h bound to bovine trypsin.