N-(4-(N-(5-methylisoxazol-3-yl)sulfamoyl)phenyl)-2-(naphthalen-2-yl)acetamide

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: N-(4-(N-(5-methylisoxazol-3-yl)sulfamoyl)phenyl)-2-(naphthalen-2-yl)acetamide
• 化学式: C₂₂H₁₉N₃O₄S
• 分子量: 421.477
• InChiKey: IGZIWEJRUCQXBT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.12
• 重原子数：
  30.0
• 可旋转键数：
  6.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.09
• 拓扑面积：
  101.3
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为产物：
  描述：

  醋磺胺甲噁唑 在 盐酸 、 N,N-二异丙基乙胺 作用下， 以 甲醇 、 乙醚 、 二氯甲烷 为溶剂， 反应 0.25h， 生成 N-(4-(N-(5-methylisoxazol-3-yl)sulfamoyl)phenyl)-2-(naphthalen-2-yl)acetamide
  参考文献：
  名称：

  Identification of ML251, a Potent Inhibitor of T. brucei and T. cruzi Phosphofructokinase

  摘要：

  Human African Trypanosomiasis (HAT) is a severe, often fatal disease caused by the parasitic protist Trypanosoma brucei. The glycolytic pathway has been identified as the sole mechanism for ATP generation in the infective stage of these organisms, and several glycolytic enzymes, phosphofructokinase (PFK) in particular, have shown promise as potential drug targets. Herein, we describe the discovery of ML251, a novel nanomolar inhibitor of T. brucei PFK, and the structure-activity relationships within the series.

  DOI：

  10.1021/ml400259d

文献信息

• Identification of ML251, a Potent Inhibitor of <i>T. brucei and T. cruzi</i> Phosphofructokinase
  作者：Kyle R. Brimacombe、Martin J. Walsh、Li Liu、Montserrat G. Vásquez-Valdivieso、Hugh P. Morgan、Iain McNae、Linda A. Fothergill-Gilmore、Paul A. M. Michels、Douglas S. Auld、Anton Simeonov、Malcolm D. Walkinshaw、Min Shen、Matthew B. Boxer

  DOI：10.1021/ml400259d

  日期：2014.1.9

  Human African Trypanosomiasis (HAT) is a severe, often fatal disease caused by the parasitic protist Trypanosoma brucei. The glycolytic pathway has been identified as the sole mechanism for ATP generation in the infective stage of these organisms, and several glycolytic enzymes, phosphofructokinase (PFK) in particular, have shown promise as potential drug targets. Herein, we describe the discovery of ML251, a novel nanomolar inhibitor of T. brucei PFK, and the structure-activity relationships within the series.