4-methylcoumarin-7-oxymethyl 6-(4-sulfamoylbenzamido)hexanoate | 1373516-78-9

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 香豆素及其衍生物
• 英文名称: 4-methylcoumarin-7-oxymethyl 6-(4-sulfamoylbenzamido)hexanoate
• 英文别名: (4-Methyl-2-oxochromen-7-yl)oxymethyl 6-[(4-sulfamoylbenzoyl)amino]hexanoate；(4-methyl-2-oxochromen-7-yl)oxymethyl 6-[(4-sulfamoylbenzoyl)amino]hexanoate
• CAS: 1373516-78-9
• 化学式: C₂₄H₂₆N₂O₈S
• 分子量: 502.545
• InChiKey: USVJZEGKSSMJPC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  35
• 可旋转键数：
  12
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  160
• 氢给体数：
  2
• 氢受体数：
  9

反应信息

• 作为产物：
  描述：

  4-methylcoumarin-7-oxymethyl 6-azidohexanoate 在 三苯基膦 、 N,N'-羰基二咪唑 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 22.33h， 生成 4-methylcoumarin-7-oxymethyl 6-(4-sulfamoylbenzamido)hexanoate
  参考文献：
  名称：

  Supramolecular Displacement-Mediated Activation of a Silent Fluorescence Probe for Label-Free Ligand Screening

  摘要：

  We report a new approach for the rapid screening of analyte binding affinities for a target protein. We demonstrate that a molecular probe, with a profluorophore substrate and ligand moieties, can be hindered from enzymatic access when bound to the target protein. When analytes displace the probe from the protein's binding pocket, a fluorescence profile is generated. This profile is used to discriminate analytes based on their relative binding affinities.

  DOI：

  10.1021/ja301204z

文献信息

• Supramolecular Displacement-Mediated Activation of a Silent Fluorescence Probe for Label-Free Ligand Screening
  作者：Diego Amado Torres、Malar A. Azagarsamy、S. Thayumanavan

  DOI：10.1021/ja301204z

  日期：2012.5.2

  We report a new approach for the rapid screening of analyte binding affinities for a target protein. We demonstrate that a molecular probe, with a profluorophore substrate and ligand moieties, can be hindered from enzymatic access when bound to the target protein. When analytes displace the probe from the protein's binding pocket, a fluorescence profile is generated. This profile is used to discriminate analytes based on their relative binding affinities.