2,2'-ethyne-1,2-diylbis(5-aminobenzenesulfonic acid) | 50567-77-6

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 二苯乙烯类
• 英文名称: 2,2'-ethyne-1,2-diylbis(5-aminobenzenesulfonic acid)
• 英文别名: 4,4'-Diamino-tolan-2,2'-disulfonsaeure；5,5'-diamino-2,2'-ethynediyl-bis-benzenesulfonic acid；5,5'-Diamino-2,2'-aethindiyl-bis-benzolsulfonsaeure；4.4'-Diamino-tolan-disulfonsaeure-(2.2')；5-Amino-2-[2-(4-amino-2-sulfophenyl)ethynyl]benzenesulfonic acid
• CAS: 50567-77-6
• 化学式: C₁₄H₁₂N₂O₆S₂
• 分子量: 368.391
• InChiKey: HFDGAAKIBOPPKP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.1
• 重原子数：
  24
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  178
• 氢给体数：
  4
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  2,2'-ethyne-1,2-diylbis(5-aminobenzenesulfonic acid) 、 氯乙酰氯 在 sodium hydroxide 作用下， 反应 1.0h， 以75%的产率得到2,2'-ethyne-1,2-diylbis{5-[(chloroacetyl)amino]benzenesulfonic acid}
  参考文献：
  名称：

  Stabilization of Folded Peptide and Protein Structures via Distance Matching with a Long, Rigid Cross-Linker

  摘要：

  Intramolecular cross-linking is predicted to stabilize the folded state of peptides and proteins most effectively if the cross-linker provides a rigid link that is well-matched in end-to-end distance with attachment sites in the peptide or protein. We describe a thiol-reactive sulfonated alkyne-based cross-linker that is demonstrably more effective than more flexible counterparts. Exceptional stabilization of helical structure in short peptides is obtained.

  DOI：

  10.1021/ja075829t
• 作为产物：
  描述：

  alkaline earth salt of/the/ methylsulfuric acid 在 盐酸 、 tin(ll) chloride 作用下， 生成 2,2'-ethyne-1,2-diylbis(5-aminobenzenesulfonic acid)
  参考文献：
  名称：

  Ruggli; Peyer, Helvetica Chimica Acta, 1926, vol. 9, p. 937

  摘要：

  DOI：

文献信息

• Ruggli; Peyer, Helvetica Chimica Acta, 1926, vol. 9, p. 937
  作者：Ruggli、Peyer

  DOI：——

  日期：——
• Stabilization of Folded Peptide and Protein Structures via Distance Matching with a Long, Rigid Cross-Linker
  作者：Fuzhong Zhang、Oleg Sadovski、Steven J. Xin、G. Andrew Woolley

  DOI：10.1021/ja075829t

  日期：2007.11.1

  Intramolecular cross-linking is predicted to stabilize the folded state of peptides and proteins most effectively if the cross-linker provides a rigid link that is well-matched in end-to-end distance with attachment sites in the peptide or protein. We describe a thiol-reactive sulfonated alkyne-based cross-linker that is demonstrably more effective than more flexible counterparts. Exceptional stabilization of helical structure in short peptides is obtained.