{2-amino-[4-(5-N-tert-butyloxycarbonylamino)pentyl]}pyrimidine | 446234-37-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: {2-amino-[4-(5-N-tert-butyloxycarbonylamino)pentyl]}pyrimidine
• CAS: 446234-37-3
• 化学式: C₁₄H₂₄N₄O₂
• 分子量: 280.37
• InChiKey: DAJPDKUKBZJRSC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  20.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  90.13
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  {2-amino-[4-(5-N-tert-butyloxycarbonylamino)pentyl]}pyrimidine 在 吡啶 、 sodium hydroxide 作用下， 生成 N1-{[4-(5-N-tert-butoxycarbonylamino)pentyl]-2-pyrimidyl}-sulfanilamide
  参考文献：
  名称：

  Improving Broad Specificity Hapten Recognition with Protein Engineering

  摘要：

  Sulfa antibiotics (sulfonamides) are derivatives of p-aminobenzenesulfonamide that are widely used in veterinary medicine. Foods derived from treated animals may be contaminated with these drugs. However, current immunobased sulfonamide detection methods are unfit for screening of products because they are either too insensitive or specific for a few compounds only. An immunoassay capable of detecting all sulfas in a single reaction would be ideal for screening. For development of a binder capable of binding all sulfas, a protein engineering approach was chosen and the properties of monoclonal antibody 27G3 were improved with mutagenesis followed by selection with phage display. Several different mutant antibodies were isolated. The cross-reaction profile of the best mutant antibody was significantly improved over that of the wild-type antibody: it was capable of binding 9 of the tested 13 sulfonamides within a narrow concentration range and also bound the rest of the sulfas, albeit within a wider concentration range.

  DOI：

  10.1021/jf0200624
• 作为产物：
  描述：

  二碳酸二叔丁酯 在 N-甲基吗啉 、 sodium hydroxide 、 三乙胺 、 氯甲酸异丁酯 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 乙醚 、 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 8.0h， 生成 {2-amino-[4-(5-N-tert-butyloxycarbonylamino)pentyl]}pyrimidine
  参考文献：
  名称：

  Improving Broad Specificity Hapten Recognition with Protein Engineering

  摘要：

  Sulfa antibiotics (sulfonamides) are derivatives of p-aminobenzenesulfonamide that are widely used in veterinary medicine. Foods derived from treated animals may be contaminated with these drugs. However, current immunobased sulfonamide detection methods are unfit for screening of products because they are either too insensitive or specific for a few compounds only. An immunoassay capable of detecting all sulfas in a single reaction would be ideal for screening. For development of a binder capable of binding all sulfas, a protein engineering approach was chosen and the properties of monoclonal antibody 27G3 were improved with mutagenesis followed by selection with phage display. Several different mutant antibodies were isolated. The cross-reaction profile of the best mutant antibody was significantly improved over that of the wild-type antibody: it was capable of binding 9 of the tested 13 sulfonamides within a narrow concentration range and also bound the rest of the sulfas, albeit within a wider concentration range.

  DOI：

  10.1021/jf0200624