4',5'-bis(1,3,2-dithioarsolan-2-yl)-2',7'-dibromofluorescein

• 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: 4',5'-bis(1,3,2-dithioarsolan-2-yl)-2',7'-dibromofluorescein
• 英文别名: 2',7'-Dibromo-4',5'-bis(1,3,2-dithiarsolan-2-yl)-3',6'-dihydroxyspiro[2-benzofuran-3,9'-xanthene]-1-one；2',7'-dibromo-4',5'-bis(1,3,2-dithiarsolan-2-yl)-3',6'-dihydroxyspiro[2-benzofuran-3,9'-xanthene]-1-one
• 化学式: C₂₄H₁₆As₂Br₂O₅S₄
• 分子量: 822.303
• InChiKey: SDRYTSXPCWYYNX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.54
• 重原子数：
  37
• 可旋转键数：
  2
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  177
• 氢给体数：
  2
• 氢受体数：
  9

反应信息

• 作为产物：
  描述：

  、 1,2-乙二硫醇 在 palladium diacetate 三氯化砷 、 N,N-二异丙基乙胺 作用下， 以 N-甲基吡咯烷酮 、 phosphate buffer 、 丙酮 为溶剂， 反应 2.0h， 生成 4',5'-bis(1,3,2-dithioarsolan-2-yl)-2',7'-dibromofluorescein
  参考文献：
  名称：

  New Biarsenical Ligands and Tetracysteine Motifs for Protein Labeling in Vitro and in Vivo:  Synthesis and Biological Applications

  摘要：

  We recently introduced a method (Griffin, B. A.; Adams, S. R.; Tsien, R. Y. Science 1998, 281, 269-272 and Griffin, B. A.; Adams, S. R.; Jones, J.; Tsien, R. Y. Methods Enzymol. 2000, 327,565-578) for site-specific fluorescent labeling of recombinant proteins in living cells. The sequence Cys-Cys-Xaa-Xaa-Cys-Cys, where Xaa is an noncysteine amino acid, is genetically fused to or inserted within the protein, where it can be specifically recognized by a membrane-permeant fluorescein derivative with two As(III) substituents, RASH, which fluoresces only after the arsenics bind to the cysteine thiols. We now report kinetics and dissociation constants (similar to10(-11) M) for FIAsH binding to model tetracysteine peptides. Affinities in vitro and detection limits in living cells are optimized with Xaa-Xaa = Pro-Gly, suggesting that the preferred peptide conformation is a hairpin rather than the previously proposed alpha-helix. Many analogues of RASH have been synthesized, including ReAsH, a resorufin derivative excitable at 590 nm and fluorescing in the red. Analogous biarsenicals enable affinity chromatography, fluorescence anisotropy measurements, and electron-microscopic localization of tetracysteine-tagged proteins.

  DOI：

  10.1021/ja017687n

文献信息

• New Biarsenical Ligands and Tetracysteine Motifs for Protein Labeling in Vitro and in Vivo:  Synthesis and Biological Applications
  作者：Stephen R. Adams、Robert E. Campbell、Larry A. Gross、Brent R. Martin、Grant K. Walkup、Yong Yao、Juan Llopis、Roger Y. Tsien

  DOI：10.1021/ja017687n

  日期：2002.5.1

  We recently introduced a method (Griffin, B. A.; Adams, S. R.; Tsien, R. Y. Science 1998, 281, 269-272 and Griffin, B. A.; Adams, S. R.; Jones, J.; Tsien, R. Y. Methods Enzymol. 2000, 327,565-578) for site-specific fluorescent labeling of recombinant proteins in living cells. The sequence Cys-Cys-Xaa-Xaa-Cys-Cys, where Xaa is an noncysteine amino acid, is genetically fused to or inserted within the protein, where it can be specifically recognized by a membrane-permeant fluorescein derivative with two As(III) substituents, RASH, which fluoresces only after the arsenics bind to the cysteine thiols. We now report kinetics and dissociation constants (similar to10(-11) M) for FIAsH binding to model tetracysteine peptides. Affinities in vitro and detection limits in living cells are optimized with Xaa-Xaa = Pro-Gly, suggesting that the preferred peptide conformation is a hairpin rather than the previously proposed alpha-helix. Many analogues of RASH have been synthesized, including ReAsH, a resorufin derivative excitable at 590 nm and fluorescing in the red. Analogous biarsenicals enable affinity chromatography, fluorescence anisotropy measurements, and electron-microscopic localization of tetracysteine-tagged proteins.