(R)-3-(5-amino-6-(1-(4-chlorophenyl)ethylamino)pyrazin-2-yl)-4-methylbenzoic acid | 1459216-49-9

• 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: (R)-3-(5-amino-6-(1-(4-chlorophenyl)ethylamino)pyrazin-2-yl)-4-methylbenzoic acid
• 英文别名: 3-[5-amino-6-[[(1R)-1-(4-chlorophenyl)ethyl]amino]pyrazin-2-yl]-4-methylbenzoic acid
• CAS: 1459216-49-9
• 化学式: C₂₀H₁₉ClN₄O₂
• 分子量: 382.849
• InChiKey: ARFUEGGWDJJGFD-GFCCVEGCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  27
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.15
• 拓扑面积：
  101
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  (R)-(+)-1-(4-氯苯基)乙胺 在 1,1'-双(二苯膦基)二茂铁二氯化钯(II)二氯甲烷复合物 、 lithium hydroxide monohydrate 、 水 、 caesium carbonate 、 N,N-二异丙基乙胺 作用下， 以 1,4-二氧六环 、 甲醇 、 水 、 正丁醇 为溶剂， 反应 9.5h， 生成 (R)-3-(5-amino-6-(1-(4-chlorophenyl)ethylamino)pyrazin-2-yl)-4-methylbenzoic acid
  参考文献：
  名称：

  Identification of 2-amino-5-aryl-pyrazines as inhibitors of human lactate dehydrogenase

  摘要：

  A 2-amino-5-aryl-pyrazine was identified as an inhibitor of human lactate dehydrogenase A (LDHA) via a biochemical screening campaign. Biochemical and biophysical experiments demonstrated that the compound specifically interacted with human LDHA. Structural variation of the screening hit resulted in improvements in LDHA biochemical inhibition and pharmacokinetic properties. A crystal structure of an improved compound bound to human LDHA was also obtained and it explained many of the observed structure-activity relationships. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.08.060

文献信息

• Identification of 2-amino-5-aryl-pyrazines as inhibitors of human lactate dehydrogenase
  作者：Benjamin P. Fauber、Peter S. Dragovich、Jinhua Chen、Laura B. Corson、Charles Z. Ding、Charles Eigenbrot、Anthony M. Giannetti、Thomas Hunsaker、Sharada Labadie、Yichin Liu、Yingchun Liu、Shiva Malek、David Peterson、Keith Pitts、Steve Sideris、Mark Ultsch、Erica VanderPorten、Jing Wang、BinQing Wei、Ivana Yen、Qin Yue

  DOI：10.1016/j.bmcl.2013.08.060

  日期：2013.10

  A 2-amino-5-aryl-pyrazine was identified as an inhibitor of human lactate dehydrogenase A (LDHA) via a biochemical screening campaign. Biochemical and biophysical experiments demonstrated that the compound specifically interacted with human LDHA. Structural variation of the screening hit resulted in improvements in LDHA biochemical inhibition and pharmacokinetic properties. A crystal structure of an improved compound bound to human LDHA was also obtained and it explained many of the observed structure-activity relationships. (C) 2013 Elsevier Ltd. All rights reserved.