6-(N-benzoyl-DL-arginylamido)quinoline | 84680-45-5

• 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: 6-(N-benzoyl-DL-arginylamido)quinoline
• 英文别名: N-[5-(diaminomethylideneamino)-1-oxo-1-(quinolin-6-ylamino)pentan-2-yl]benzamide
• CAS: 84680-45-5
• 化学式: C₂₂H₂₄N₆O₂
• 分子量: 404.472
• InChiKey: ZNLJLXZVPJDUOT-UHFFFAOYSA-N

物化性质

• 密度：
  1.31±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.6
• 重原子数：
  30
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  136
• 氢给体数：
  4
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  6-(N-benzoyl-DL-arginylamido)quinoline 、 碘甲烷 以 N,N-二甲基甲酰胺 为溶剂， 反应 48.0h， 以62%的产率得到1-methyl-6-(N-benzoyl-DL-arginylamido)quinolinium diiodide
  参考文献：
  名称：

  Synthesis and kinetic studies of protease substrates containing the 1-methyl-6-aminoquinolinium ion as a fluorogenic leaving group

  摘要：

  Several sensitive substrates for porcine pancreatic elastase, chymotrypsin, and trypsin were prepared that utilize the permanently charged, fluorogenic cation 1-methyl-6-aminoquinoline (MAQ+) as the leaving group. Kinetic rates for the hydrolysis of substrates were determined fluorimetrically and compared with analogues having 6-aminoquinoline (6-AQ) as an uncharged leaving group. It was found that substrates containing the quaternized leaving group generally have a higher kcat/Km ratio. An exception to this trend was noted with a trypsin substrate, Bz-DL-Arg-MAQ+. During the course of this investigation, several significant advantages of the MAQ+ ion as a fluorogenic leaving group in protease substrates were found: (a) its appearance can be measured fluorimetrically using wavelengths of light that result in its maximal fluorescence, while under these conditions, the unhydrolyzed substrate is essentially nonfluorescent, (b) it confers a high degree of water solubility to hydrophobic peptides, thereby eliminating the need for organic cosolvents to dissolve substrates, and (c) quaternized substrates can be prepared readily and in good yield from the corresponding 6-(peptidylamido)quinolines. These positively charged synthetic fluorogenic substrates are, therefore, useful probes for investigating the steric and electronic properties of the active-site environment of proteolytic enzymes.

  DOI：

  10.1021/jm00375a014
• 作为产物：
  描述：

  6-氨基喹啉 在 甲烷磺酸 、 苯甲醚 、 三乙胺 、 氯甲酸异丁酯 作用下， 反应 25.42h， 生成 6-(N-benzoyl-DL-arginylamido)quinoline
  参考文献：
  名称：

  Synthesis and kinetic studies of protease substrates containing the 1-methyl-6-aminoquinolinium ion as a fluorogenic leaving group

  摘要：

  Several sensitive substrates for porcine pancreatic elastase, chymotrypsin, and trypsin were prepared that utilize the permanently charged, fluorogenic cation 1-methyl-6-aminoquinoline (MAQ+) as the leaving group. Kinetic rates for the hydrolysis of substrates were determined fluorimetrically and compared with analogues having 6-aminoquinoline (6-AQ) as an uncharged leaving group. It was found that substrates containing the quaternized leaving group generally have a higher kcat/Km ratio. An exception to this trend was noted with a trypsin substrate, Bz-DL-Arg-MAQ+. During the course of this investigation, several significant advantages of the MAQ+ ion as a fluorogenic leaving group in protease substrates were found: (a) its appearance can be measured fluorimetrically using wavelengths of light that result in its maximal fluorescence, while under these conditions, the unhydrolyzed substrate is essentially nonfluorescent, (b) it confers a high degree of water solubility to hydrophobic peptides, thereby eliminating the need for organic cosolvents to dissolve substrates, and (c) quaternized substrates can be prepared readily and in good yield from the corresponding 6-(peptidylamido)quinolines. These positively charged synthetic fluorogenic substrates are, therefore, useful probes for investigating the steric and electronic properties of the active-site environment of proteolytic enzymes.

  DOI：

  10.1021/jm00375a014

文献信息

• Synthesis and kinetic studies of protease substrates containing the 1-methyl-6-aminoquinolinium ion as a fluorogenic leaving group
  作者：Patricia Andrade-Gordon、David Gordon、Paul J. Brynes、Cheng Wen Wu

  DOI：10.1021/jm00375a014

  日期：1984.9

  Several sensitive substrates for porcine pancreatic elastase, chymotrypsin, and trypsin were prepared that utilize the permanently charged, fluorogenic cation 1-methyl-6-aminoquinoline (MAQ+) as the leaving group. Kinetic rates for the hydrolysis of substrates were determined fluorimetrically and compared with analogues having 6-aminoquinoline (6-AQ) as an uncharged leaving group. It was found that substrates containing the quaternized leaving group generally have a higher kcat/Km ratio. An exception to this trend was noted with a trypsin substrate, Bz-DL-Arg-MAQ+. During the course of this investigation, several significant advantages of the MAQ+ ion as a fluorogenic leaving group in protease substrates were found: (a) its appearance can be measured fluorimetrically using wavelengths of light that result in its maximal fluorescence, while under these conditions, the unhydrolyzed substrate is essentially nonfluorescent, (b) it confers a high degree of water solubility to hydrophobic peptides, thereby eliminating the need for organic cosolvents to dissolve substrates, and (c) quaternized substrates can be prepared readily and in good yield from the corresponding 6-(peptidylamido)quinolines. These positively charged synthetic fluorogenic substrates are, therefore, useful probes for investigating the steric and electronic properties of the active-site environment of proteolytic enzymes.