1-[3-Methyl-4-(Piperidin-4-Yloxy)-1-Benzofuran-2-Yl]-3-Phenylpropan-1-One | 1402930-17-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并呋喃
• 英文名称: 1-[3-Methyl-4-(Piperidin-4-Yloxy)-1-Benzofuran-2-Yl]-3-Phenylpropan-1-One
• 英文别名: 1-(3-methyl-4-piperidin-4-yloxy-1-benzofuran-2-yl)-3-phenylpropan-1-one
• CAS: 1402930-17-9
• 化学式: C₂₃H₂₅NO₃
• 分子量: 363.456
• InChiKey: ZUAGYVKWPGUWFU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.7
• 重原子数：
  27
• 可旋转键数：
  6
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  51.5
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  tert-butyl 4-[(2-acetyl-3-methyl-1-benzofuran-4-yl)oxy]piperidine-1-carboxylate 在 1,4-环己二烯 、 palladium 10% on activated carbon 、 三氟乙酸 、 sodium hydroxide 作用下， 以 乙醇 、 二氯甲烷 为溶剂， 反应 9.0h， 生成 1-[3-Methyl-4-(Piperidin-4-Yloxy)-1-Benzofuran-2-Yl]-3-Phenylpropan-1-One
  参考文献：
  名称：

  Design and Synthesis of Inhibitors of Plasmodium falciparumN-Myristoyltransferase, A Promising Target for Antimalarial Drug Discovery

  摘要：

  Design of inhibitors for N-myristoyltransferase (NMT), an enzyme responsible for protein trafficking in Plasmodium falciparum, the most lethal species of parasites that cause malaria, is described. Chemistry-driven optimization of compound 1 from a focused NMT inhibitor library led to the identification of two early lead compounds 4 and 25, which showed good enzyme and cellular potency and excellent selectivity over human NMT. These molecules provide a valuable starting point for further development.

  DOI：

  10.1021/jm301160h

文献信息

• Design and Synthesis of Inhibitors of <i>Plasmodium falciparumN</i>-Myristoyltransferase, A Promising Target for Antimalarial Drug Discovery
  作者：Zhiyong Yu、James A. Brannigan、David K. Moss、A. Marek Brzozowski、Anthony J. Wilkinson、Anthony A. Holder、Edward W. Tate、Robin J. Leatherbarrow

  DOI：10.1021/jm301160h

  日期：2012.10.25

  Design of inhibitors for N-myristoyltransferase (NMT), an enzyme responsible for protein trafficking in Plasmodium falciparum, the most lethal species of parasites that cause malaria, is described. Chemistry-driven optimization of compound 1 from a focused NMT inhibitor library led to the identification of two early lead compounds 4 and 25, which showed good enzyme and cellular potency and excellent selectivity over human NMT. These molecules provide a valuable starting point for further development.