N-(4-hydroxyphenyl)-4-methylpentanamide | 1042641-58-6

• 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: N-(4-hydroxyphenyl)-4-methylpentanamide
• CAS: 1042641-58-6
• 化学式: C₁₂H₁₇NO₂
• 分子量: 207.272
• InChiKey: JLHIBCQXSKCXDT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  15
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  49.3
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  4-甲基戊酸 、 对氨基苯酚 在 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 生成 N-(4-hydroxyphenyl)-4-methylpentanamide
  参考文献：
  名称：

  Fenretinide Derivatives Act as Disrupters of Interactions of Serum Retinol Binding Protein (sRBP) with Transthyretin and the sRBP Receptor

  摘要：

  Serum retinol binding protein (sRBP) is released from the liver as a complex with transthyretin (TTR), a process under the control of dietary retinol. Elevated levels of sRBP may be involved in inhibiting cellular responses to insulin and in generating first insulin resistance and then type 2 diabetes, offering a new target for therapeutic attack for these conditions. A series of retinoid analogues were synthesized and examined for their binding to sRBP and their ability to disrupt the sRBP-TTR and sRBP-sRBP receptor interactions. A number inhibit the sRBP-TTR and sRBP-sRBP receptor interactions as well as or better than Fenretinide (FEN), presenting a potential novel dual mechanism of action and perhaps offering a new therapeutic intervention against type 2 diabetes and its development. Shortening the chain length of the FEN derivative substantially abolished binding to sRBP, indicating that the strength of the interaction the polyene chain region. Differences in potency against the sRBP-TTR and sRBP-sRBP receptor interactions suggest variant effects of the compounds on the two loops of sRBP guarding the entrance of the binding pocket that are responsible for these two protein-protein interactions.

  DOI：

  10.1021/jm200256g

文献信息

• C(sp³)–C(sp³) coupling of non-activated alkyl-iodides with electron-deficient alkenes <i>via</i> visible-light/silane-mediated alkyl-radical formation
  作者：Sanesh Mistry、Roopender Kumar、Andrew Lister、Matthew J. Gaunt

  DOI：10.1039/d2sc03516b

  日期：——

  Here, we present a remarkably mild and general initiation protocol for alkyl-radical generation from non-activated alkyl-iodides. An interaction between a silane and an alkyl iodide is excited by irradiation with visible light to trigger carbon–iodide bond homolysis and form the alkyl radical. We show how this method can be developed into an operationally simple and general Giese addition reaction

  在这里，我们提出了一个非常温和和通用的启动协议，用于从非活化的烷基碘化物中产生烷基自由基。可见光照射可激发硅烷和烷基碘之间的相互作用，引发碳-碘化物键均裂并形成烷基自由基。我们展示了如何将这种方法发展成一种操作简单且通用的 Giese 加成反应，该反应可以容忍一系列敏感的功能，而这些功能通常不会在这种具有战略意义的重要转变的既定方法中探索。新方法不需要光催化剂或其他添加剂，仅使用商业三（三甲基甲硅烷基）硅烷和可见光即可有效地将多种烷基卤化物与活化烯烃结合形成 C(sp 3 )–C(sp 3) 嵌入复杂框架中的债券。
• Fenretinide Derivatives Act as Disrupters of Interactions of Serum Retinol Binding Protein (sRBP) with Transthyretin and the sRBP Receptor
  作者：José Angel Campos-Sandoval、Clara Redondo、Gemma K. Kinsella、Akos Pal、Geraint Jones、Gwen S. Eyre、Simon C. Hirst、John B. C. Findlay

  DOI：10.1021/jm200256g

  日期：2011.7.14

  Serum retinol binding protein (sRBP) is released from the liver as a complex with transthyretin (TTR), a process under the control of dietary retinol. Elevated levels of sRBP may be involved in inhibiting cellular responses to insulin and in generating first insulin resistance and then type 2 diabetes, offering a new target for therapeutic attack for these conditions. A series of retinoid analogues were synthesized and examined for their binding to sRBP and their ability to disrupt the sRBP-TTR and sRBP-sRBP receptor interactions. A number inhibit the sRBP-TTR and sRBP-sRBP receptor interactions as well as or better than Fenretinide (FEN), presenting a potential novel dual mechanism of action and perhaps offering a new therapeutic intervention against type 2 diabetes and its development. Shortening the chain length of the FEN derivative substantially abolished binding to sRBP, indicating that the strength of the interaction the polyene chain region. Differences in potency against the sRBP-TTR and sRBP-sRBP receptor interactions suggest variant effects of the compounds on the two loops of sRBP guarding the entrance of the binding pocket that are responsible for these two protein-protein interactions.