QSY7-maleimide | 648881-03-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• 英文名称: QSY7-maleimide
• 英文别名: [9-[2-[4-[5-(2,5-dioxopyrrol-1-yl)pentylcarbamoyl]piperidin-1-yl]sulfonylphenyl]-6-(N-methylanilino)xanthen-3-ylidene]-methyl-phenylazanium
• CAS: 648881-03-2
• 化学式: C₄₈H₄₈N₅O₆S
• 分子量: 823.005
• InChiKey: PZBRLKNFIFOXIX-UHFFFAOYSA-O

计算性质

• 辛醇/水分配系数(LogP)：
  6
• 重原子数：
  60
• 可旋转键数：
  13
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  128
• 氢给体数：
  1
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  QSY7-maleimide 、 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 生成
  参考文献：
  名称：

  Light-Mediated Spatial Control via Photolabile Fluorescently Quenched Peptide Cassettes

  摘要：

  Light-regulatable compounds are finding increasing utility as spatial and temporal probes of biological behavior. An independent measure Of Successful light-induced structural change is possible when alteration (e.g., activation, deactivation, etc.) of the bioprobe can be directly linked to a fluorescent readout. We have identified a series of photolabile fluorescently quenched cassettes that display extraordinarily large fluorescence enhancements upon photolysis. A pair of cassettes has been inserted into mitochondrial localization sequences to assess an organ e I I e-targeted light-mediated release strategy for controlling biological activity. The peptide constructs are readily absorbed by mitochondria and subsequently can be cleaved in a light-dependent fashion as assessed by the predicted changes in absorbance and fluorescence.

  DOI：

  10.1021/ja907427p

文献信息

• Construction of a Photoactivatable Profluorescent Enzyme Via Propinquity Labeling
  作者：Hsien-Ming Lee、Weichen Xu、David S. Lawrence

  DOI：10.1021/ja108950q

  日期：2011.3.2

  A strategy for the construction of a profluorescent caged enzyme is described. An active site-directed peptide-based affinity label was designed, synthesized, and employed to covalently label a nonactive site residue in the cAMP-dependent protein kinase. The modified kinase displays minimal catalytic activity and low fluorescence. Photolysis results in partial cleavage of the enzyme-bound affinity label, restoration of enzymatic activity (60-80%) and a strong fluorescent response (10-20 fold). The caged kinase displays analogous behavior in living cells, inducing a light-dependent loss of stress fibers that is characteristic of cAMP action. This strategy furnishes molecularly engineered enzymes that can be remotely controlled in time space, and total activity.