3-(3-methoxy-5-(2,6-diisopropylphenyl)phenyl)butyne | 1073642-99-5

• 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-methoxy-5-(2,6-diisopropylphenyl)phenyl)butyne
• 英文别名: 1-But-3-yn-2-yl-3-[2,6-di(propan-2-yl)phenyl]-5-methoxybenzene
• CAS: 1073642-99-5
• 化学式: C₂₃H₂₈O
• 分子量: 320.475
• InChiKey: JXQLKQSCDXJIRK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.6
• 重原子数：
  24
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  9.2
• 氢给体数：
  0
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  3-(3-methoxy-5-(2,6-diisopropylphenyl)phenyl)butyne 、 5-碘-6-甲基嘧啶-2,4-二胺 在 bis-triphenylphosphine-palladium(II) chloride 、 copper(l) iodide 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 3.5h， 以67%的产率得到2,4-diamino-5-[3-(3-methoxy-5-(2,6-diisopropylphenyl)phenyl)but-1-ynyl]-6-methylpyrimidine
  参考文献：
  名称：

  Structure-Based Approach to the Development of Potent and Selective Inhibitors of Dihydrofolate Reductase from Cryptosporidium

  摘要：

  Cryptosporidiosis is an emerging infectious disease that can be life-threatening in ail immune-compromised individual and causes gastrointestinal distress lasting up to 2 weeks in an immune-competent individual. There are few therapeutics available for effectively treating this disease. We have been exploring dihydrofolate reductase (DHFR) as a potential target in Cryptosporidium. On the basis of the structure of the DHFR enzyme from C. hominis, we have developed a novel scaffold that led to the discovery of potent (38 nM) and efficient inhibitors of this enzyme. Recently, we have advanced these inhibitors to the next stage of development. Using the Structures of both the protozoal and human enzymes. we have developed inhibitors with nanomolar potency (1.1 nM) against the pathogenic enzyme and high levels (1273-fold) of selectivity over the human enzyme.

  DOI：

  10.1021/jm8009124
• 作为产物：
  描述：

  2-(3-methoxy-5-(2,6-diisopropylphenyl)phenyl)propanal 、 (1-重氮基-2-氧代丙基)膦酸二甲酯 在 potassium carbonate 作用下， 以 甲醇 为溶剂， 反应 1.5h， 以80%的产率得到3-(3-methoxy-5-(2,6-diisopropylphenyl)phenyl)butyne
  参考文献：
  名称：

  Structure-Based Approach to the Development of Potent and Selective Inhibitors of Dihydrofolate Reductase from Cryptosporidium

  摘要：

  Cryptosporidiosis is an emerging infectious disease that can be life-threatening in ail immune-compromised individual and causes gastrointestinal distress lasting up to 2 weeks in an immune-competent individual. There are few therapeutics available for effectively treating this disease. We have been exploring dihydrofolate reductase (DHFR) as a potential target in Cryptosporidium. On the basis of the structure of the DHFR enzyme from C. hominis, we have developed a novel scaffold that led to the discovery of potent (38 nM) and efficient inhibitors of this enzyme. Recently, we have advanced these inhibitors to the next stage of development. Using the Structures of both the protozoal and human enzymes. we have developed inhibitors with nanomolar potency (1.1 nM) against the pathogenic enzyme and high levels (1273-fold) of selectivity over the human enzyme.

  DOI：

  10.1021/jm8009124

文献信息

• Structure-Based Approach to the Development of Potent and Selective Inhibitors of Dihydrofolate Reductase from <i>Cryptosporidium</i>
  作者：David B. Bolstad、Erin S. D. Bolstad、Kathleen M. Frey、Dennis L. Wright、Amy C. Anderson

  DOI：10.1021/jm8009124

  日期：2008.11.13

  Cryptosporidiosis is an emerging infectious disease that can be life-threatening in ail immune-compromised individual and causes gastrointestinal distress lasting up to 2 weeks in an immune-competent individual. There are few therapeutics available for effectively treating this disease. We have been exploring dihydrofolate reductase (DHFR) as a potential target in Cryptosporidium. On the basis of the structure of the DHFR enzyme from C. hominis, we have developed a novel scaffold that led to the discovery of potent (38 nM) and efficient inhibitors of this enzyme. Recently, we have advanced these inhibitors to the next stage of development. Using the Structures of both the protozoal and human enzymes. we have developed inhibitors with nanomolar potency (1.1 nM) against the pathogenic enzyme and high levels (1273-fold) of selectivity over the human enzyme.