tert-butyl 2-(4',5'-bis(1,3,2-dithiaarsolan-2-yl)-3',6'-dihydroxy-3-oxospiro[isoindoline-1,9'-xanthene]-2-yl) ethylcarbamate | 1028052-15-4

• 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: tert-butyl 2-(4',5'-bis(1,3,2-dithiaarsolan-2-yl)-3',6'-dihydroxy-3-oxospiro[isoindoline-1,9'-xanthene]-2-yl) ethylcarbamate
• CAS: 1028052-15-4
• 化学式: C₃₁H₃₂As₂N₂O₆S₄
• 分子量: 806.712
• InChiKey: MAPXITVGOFQIFE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.83
• 重原子数：
  45.0
• 可旋转键数：
  5.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  108.33
• 氢给体数：
  3.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  tert-butyl 2-(4',5'-bis(1,3,2-dithiaarsolan-2-yl)-3',6'-dihydroxy-3-oxospiro[isoindoline-1,9'-xanthene]-2-yl) ethylcarbamate 在 三乙胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 3.0h， 生成 N-(2-(4',5'-di(1,3,2-dithiarsolan-2-yl)-3',6'-dihydroxy-3-oxospiro[isoindoline-1,9'-xanthene]-2-yl)ethyl)-6-(5-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamido)hexanamide
  参考文献：
  名称：

  Purification of Tetracysteine-Tagged Proteins by Affinity Chromatography Using a Non-Fluorescent, Photochemically Stable Bisarsenical Affinity Ligand

  摘要：

  The use of genetically encoded small peptide tags such as polyhistidine and tetracysteine tags has become important for protein purification and enrichment. An improved affinity purification of tetracysteine (CCXXCC) tagged proteins has been achieved using a nonfluorescent, photochemically stable bisarsenical affinity ligand SplAsH. The photochemical stability of the SplAsH-biotin, shown in compound 5, is superior to FlAsH-EDT2 and ReAsH-EDT2. An application of the SplAsH tag for affinity purification of tetracysteine-tagged proteins is reported.

  DOI：

  10.1021/bc200038t
• 作为产物：
  描述：

  tert-butyl 2-(3',6'-dihydroxy-3-oxospiro[isoindoline-1,9'-xanthene]-2-yl) ethylcarbamate 在 mercury(II) diacetate 、 溶剂黄146 作用下， 以 四氢呋喃 、 乙醇 、 水 、 丙酮 为溶剂， 反应 2.5h， 生成 tert-butyl 2-(4',5'-bis(1,3,2-dithiaarsolan-2-yl)-3',6'-dihydroxy-3-oxospiro[isoindoline-1,9'-xanthene]-2-yl) ethylcarbamate
  参考文献：
  名称：

  Purification of Tetracysteine-Tagged Proteins by Affinity Chromatography Using a Non-Fluorescent, Photochemically Stable Bisarsenical Affinity Ligand

  摘要：

  The use of genetically encoded small peptide tags such as polyhistidine and tetracysteine tags has become important for protein purification and enrichment. An improved affinity purification of tetracysteine (CCXXCC) tagged proteins has been achieved using a nonfluorescent, photochemically stable bisarsenical affinity ligand SplAsH. The photochemical stability of the SplAsH-biotin, shown in compound 5, is superior to FlAsH-EDT2 and ReAsH-EDT2. An application of the SplAsH tag for affinity purification of tetracysteine-tagged proteins is reported.

  DOI：

  10.1021/bc200038t

文献信息

• WO2008/109464
  申请人：——

  公开号：——

  公开（公告）日：——