Methyl 2-amino-4-(3-cyanophenyl)butanoate | 202208-81-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: Methyl 2-amino-4-(3-cyanophenyl)butanoate
• CAS: 202208-81-9
• 化学式: C₁₂H₁₄N₂O₂
• 分子量: 218.255
• InChiKey: AMHOTVUEVCYEAM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  16
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  76.1
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Methyl 2-amino-4-(3-cyanophenyl)butanoate 在 sodium hydroxide 、 sodium tetrahydroborate 、 草酰氯 、 水 、 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 二甲基亚砜 、 三乙胺 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 4.36h， 生成 N-[4-(3-cyanophenyl)-1-oxobutan-2-yl]-4-phenylbenzamide
  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：

  间溴苯甲腈 在 Lindlar's catalyst 哌啶 、 chromium(VI) oxide 、 四(三苯基膦)钯 、 硫酸 、 2,4,6-三异丙基苯磺酰叠氮化物 、 氢气 、 lithium hexamethyldisilazane 作用下， 以 乙醚 、 乙醇 、 丙酮 为溶剂， -78.0~80.0 ℃ 、310.27 kPa 条件下， 反应 6.5h， 生成 Methyl 2-amino-4-(3-cyanophenyl)butanoate
  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.