[2-(2,4-Disulfooxyphenyl)-4-oxo-3,5-disulfooxy-chromen-7-yl] hydrogen sulfate

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 黄酮类化合物
• 英文名称: [2-(2,4-Disulfooxyphenyl)-4-oxo-3,5-disulfooxy-chromen-7-yl] hydrogen sulfate
• 英文别名: [2-(2,4-disulfooxyphenyl)-4-oxo-3,5-disulfooxychromen-7-yl] hydrogen sulfate
• 化学式: C₁₅H₁₀O₂₂S₅
• 分子量: 702.561
• InChiKey: IKEYWTBKFMCCCY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.4
• 重原子数：
  42
• 可旋转键数：
  11
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  386
• 氢给体数：
  5
• 氢受体数：
  22

反应信息

• 作为产物：
  描述：

  桑色素 在 三氧化硫-三乙胺复合物 作用下， 以 N,N-二甲基乙酰胺 为溶剂， 反应 3.0h， 生成 [2-(2,4-Disulfooxyphenyl)-4-oxo-3,5-disulfooxy-chromen-7-yl] hydrogen sulfate
  参考文献：
  名称：

  Exploring new non-sugar sulfated molecules as activators of antithrombin

  摘要：

  New non-sugar, small. sulfated molecules. based on our de novo rationally designed activator (-)-epicatechin sulfate (ECS), were investigated to bind and activate antithrombin, an inhibitor of plasma coagulation enzyme factor Xa, For the activators studied, the equilibrium dissociation constant (K-D) of the interaction,with plasma antithrombin varies nearly 53-fold, with the highest affinity of 1.8 muM observed for morin sulfate, while the acceleration in factor Xa inhibition varies 2.6-fold. The results demonstrate Lit antithrombin binding and activation is a common property of these small sulfated molecules and suggests plausible directions for designing more potent activators. (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(02)01055-7

文献信息

• Exploring new non-sugar sulfated molecules as activators of antithrombin
  作者：Gunnar T Gunnarsson、Umesh R Desai

  DOI：10.1016/s0960-894x(02)01055-7

  日期：2003.2

  New non-sugar, small. sulfated molecules. based on our de novo rationally designed activator (-)-epicatechin sulfate (ECS), were investigated to bind and activate antithrombin, an inhibitor of plasma coagulation enzyme factor Xa, For the activators studied, the equilibrium dissociation constant (K-D) of the interaction,with plasma antithrombin varies nearly 53-fold, with the highest affinity of 1.8 muM observed for morin sulfate, while the acceleration in factor Xa inhibition varies 2.6-fold. The results demonstrate Lit antithrombin binding and activation is a common property of these small sulfated molecules and suggests plausible directions for designing more potent activators. (C) 2003 Elsevier Science Ltd. All rights reserved.