4-methoxy-1-naphthyl hydrogen glutarate | 1282527-69-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 4-methoxy-1-naphthyl hydrogen glutarate
• 英文别名: 5-(4-Methoxynaphthalen-1-yl)oxy-5-oxopentanoic acid；5-(4-methoxynaphthalen-1-yl)oxy-5-oxopentanoic acid
• CAS: 1282527-69-8
• 化学式: C₁₆H₁₆O₅
• 分子量: 288.3
• InChiKey: DOOSDBIFGLJIPZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  21
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  72.8
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  4-methoxy-1-naphthyl hydrogen glutarate 生成 4-(1-hydroxy-4-methoxy-2-naphthyl)-4-oxopentanoic acid
  参考文献：
  名称：

  Site-Dependent Photo-Fries Rearrangement within Serum Albumins

  摘要：

  In the present work, the influence of serum albumins as biological hosts on the well-established photo-Fries rearrangement has been investigated. For this purpose, 4-methoxy-1-naphthyl hydrogen succinate and glutarate (1a,b) as well as the corresponding acetate (1c), have been selected as substrates. Special attention has been devoted to the effect of the binding site location and serum albumin species on the outcome of the reaction. In a first stage, the stabilizing effect of the biomacromolecule on the intramolecularly catalyzed hydrolysis of succinate 1a was observed. Then, 1b and 1c were considered for their interaction with proteins in site II and site I, respectively. Site assignment was confirmed by fluorescence displacement experiments with dansylamide and dansylglycine. Moreover, spectroscopic analysis showed a site dependent quantum yield of product formation for human and bovine serum albumin.

  DOI：

  10.1021/jp2009463
• 作为产物：
  描述：

  戊二酸酐 、 4-甲氧基-1-萘酚 在 sodium hydroxide 作用下， 以 水 为溶剂， 反应 0.08h， 生成 4-methoxy-1-naphthyl hydrogen glutarate
  参考文献：
  名称：

  Site-Dependent Photo-Fries Rearrangement within Serum Albumins

  摘要：

  In the present work, the influence of serum albumins as biological hosts on the well-established photo-Fries rearrangement has been investigated. For this purpose, 4-methoxy-1-naphthyl hydrogen succinate and glutarate (1a,b) as well as the corresponding acetate (1c), have been selected as substrates. Special attention has been devoted to the effect of the binding site location and serum albumin species on the outcome of the reaction. In a first stage, the stabilizing effect of the biomacromolecule on the intramolecularly catalyzed hydrolysis of succinate 1a was observed. Then, 1b and 1c were considered for their interaction with proteins in site II and site I, respectively. Site assignment was confirmed by fluorescence displacement experiments with dansylamide and dansylglycine. Moreover, spectroscopic analysis showed a site dependent quantum yield of product formation for human and bovine serum albumin.

  DOI：

  10.1021/jp2009463

文献信息

• Site-Dependent Photo-Fries Rearrangement within Serum Albumins
  作者：Mireia Marin、Virginie Lhiaubet-Vallet、Miguel Angel Miranda

  DOI：10.1021/jp2009463

  日期：2011.3.31

  In the present work, the influence of serum albumins as biological hosts on the well-established photo-Fries rearrangement has been investigated. For this purpose, 4-methoxy-1-naphthyl hydrogen succinate and glutarate (1a,b) as well as the corresponding acetate (1c), have been selected as substrates. Special attention has been devoted to the effect of the binding site location and serum albumin species on the outcome of the reaction. In a first stage, the stabilizing effect of the biomacromolecule on the intramolecularly catalyzed hydrolysis of succinate 1a was observed. Then, 1b and 1c were considered for their interaction with proteins in site II and site I, respectively. Site assignment was confirmed by fluorescence displacement experiments with dansylamide and dansylglycine. Moreover, spectroscopic analysis showed a site dependent quantum yield of product formation for human and bovine serum albumin.