3-(3-cyanophenyl)propionic acid thiopyridyl ester | 193151-12-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 3-(3-cyanophenyl)propionic acid thiopyridyl ester
• 英文别名: S-pyridin-2-yl 3-(3-cyanophenyl)propanethioate
• CAS: 193151-12-1
• 化学式: C₁₅H₁₂N₂OS
• 分子量: 268.339
• InChiKey: MAVSWFDDJHDQPT-UHFFFAOYSA-N

物化性质

• 沸点：
  463.3±30.0 °C(Predicted)
• 密度：
  1.25±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  19
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  79
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-(4-Methoxyphenyl)-3-phenylpropenaldimine 、 3-(3-cyanophenyl)propionic acid thiopyridyl ester 在 四氯化钛 、 三乙胺 作用下， 生成 3-[(3S,4R)-1-(4-Methoxy-phenyl)-2-oxo-4-((E)-styryl)-azetidin-3-ylmethyl]-benzonitrile 、 3-[[(3R,4R)-1-(4-methoxyphenyl)-2-oxo-4-[(E)-2-phenylethenyl]azetidin-3-yl]methyl]benzonitrile
  参考文献：
  名称：

  Identification and Initial Structure−Activity Relationships of a Novel Class of Nonpeptide Inhibitors of Blood Coagulation Factor Xa

  摘要：

  The discovery and some of the basic structure-activity relationships of a series of novel nonpeptide inhibitors of blood coagulation Factor Xa is described. These inhibitors are functionalized p-alanines, exemplified by 2a. Docking experiments placing 2a in the active site of Factor Xa implied that the Most expeditious route to enhancing in vitro potency was to modify the group occupying the S3 site of the enzyme. Increasing the hydrophobic contacts between the inhibitor and the enzyme in this region led to 8, which has served as the prototype for this series. In addition, an enantioselective synthesis of these substituted p-alanines was also developed.

  DOI：

  10.1021/jm970482y
• 作为产物：
  描述：

  3-氰基苯丙酸 在 草酰氯 、 三乙胺 、 N,N-二甲基甲酰胺 作用下， 以 二氯甲烷 为溶剂， 反应 2.0h， 生成 3-(3-cyanophenyl)propionic acid thiopyridyl ester
  参考文献：
  名称：

  Identification and Initial Structure−Activity Relationships of a Novel Class of Nonpeptide Inhibitors of Blood Coagulation Factor Xa

  摘要：

  The discovery and some of the basic structure-activity relationships of a series of novel nonpeptide inhibitors of blood coagulation Factor Xa is described. These inhibitors are functionalized p-alanines, exemplified by 2a. Docking experiments placing 2a in the active site of Factor Xa implied that the Most expeditious route to enhancing in vitro potency was to modify the group occupying the S3 site of the enzyme. Increasing the hydrophobic contacts between the inhibitor and the enzyme in this region led to 8, which has served as the prototype for this series. In addition, an enantioselective synthesis of these substituted p-alanines was also developed.

  DOI：

  10.1021/jm970482y

文献信息

• Identification and Initial Structure−Activity Relationships of a Novel Class of Nonpeptide Inhibitors of Blood Coagulation Factor Xa
  作者：Scott I. Klein、Mark Czekaj、Charles J. Gardner、Kevin R. Guertin、Daniel L. Cheney、Alfred P. Spada、Scott A. Bolton、Karen Brown、Dennis Colussi、Christopher L. Heran、Suzanne R. Morgan、Robert J. Leadley、Christopher T. Dunwiddie、Mark H. Perrone、Valeria Chu

  DOI：10.1021/jm970482y

  日期：1998.2.1

  The discovery and some of the basic structure-activity relationships of a series of novel nonpeptide inhibitors of blood coagulation Factor Xa is described. These inhibitors are functionalized p-alanines, exemplified by 2a. Docking experiments placing 2a in the active site of Factor Xa implied that the Most expeditious route to enhancing in vitro potency was to modify the group occupying the S3 site of the enzyme. Increasing the hydrophobic contacts between the inhibitor and the enzyme in this region led to 8, which has served as the prototype for this series. In addition, an enantioselective synthesis of these substituted p-alanines was also developed.