{[4-(3,5-Bis-{4-[(bis-ethoxycarbonylmethyl-amino)-methyl]-phenoxymethyl}-benzyloxy)-benzyl]-ethoxycarbonylmethyl-amino}-acetic acid ethyl ester | 352689-25-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: {[4-(3,5-Bis-{4-[(bis-ethoxycarbonylmethyl-amino)-methyl]-phenoxymethyl}-benzyloxy)-benzyl]-ethoxycarbonylmethyl-amino}-acetic acid ethyl ester
• CAS: 352689-25-9
• 化学式: C₅₄H₆₉N₃O₁₅
• 分子量: 1000.15
• InChiKey: RFHLBASAYNQDAG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.21
• 重原子数：
  72.0
• 可旋转键数：
  33.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  195.21
• 氢给体数：
  0.0
• 氢受体数：
  18.0

反应信息

• 作为反应物：
  描述：

  {[4-(3,5-Bis-{4-[(bis-ethoxycarbonylmethyl-amino)-methyl]-phenoxymethyl}-benzyloxy)-benzyl]-ethoxycarbonylmethyl-amino}-acetic acid ethyl ester 在 lithium hydroxide 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 12.0h， 以87%的产率得到{[4-(3,5-Bis-{4-[(bis-carboxymethyl-amino)-methyl]-phenoxymethyl}-benzyloxy)-benzyl]-carboxymethyl-amino}-acetic acid
  参考文献：
  名称：

  Surface Recognition of a Protein Using Designed Transition Metal Complexes

  摘要：

  Each protein has a unique pattern of histidine residues on the surface. This paper describes the design, synthesis, and binding studies of transition metal complexes to target the surface histidine pattern of carbonic anhydrase (bovine erythrocyte). When the pattern of cupric ions on a complex matches the surface pattern of histidines of the protein, strong and selective binding can be achieved in aqueous buffer (pH = 7.0). The described method of protein recognition is applicable to proteins of known structures. With rapidly increasing number of solved protein structures, the method has wide applicability in purification, targeting, and sensing of proteins.

  DOI：

  10.1021/ja003193z
• 作为产物：
  描述：

  {4-[3,5-Bis-(4-hydroxymethyl-phenoxymethyl)-benzyloxy]-phenyl}-methanol 在 三溴化磷 、 potassium carbonate 作用下， 以 乙醚 、 乙腈 为溶剂， 反应 54.0h， 生成 {[4-(3,5-Bis-{4-[(bis-ethoxycarbonylmethyl-amino)-methyl]-phenoxymethyl}-benzyloxy)-benzyl]-ethoxycarbonylmethyl-amino}-acetic acid ethyl ester
  参考文献：
  名称：

  Surface Recognition of a Protein Using Designed Transition Metal Complexes

  摘要：

  Each protein has a unique pattern of histidine residues on the surface. This paper describes the design, synthesis, and binding studies of transition metal complexes to target the surface histidine pattern of carbonic anhydrase (bovine erythrocyte). When the pattern of cupric ions on a complex matches the surface pattern of histidines of the protein, strong and selective binding can be achieved in aqueous buffer (pH = 7.0). The described method of protein recognition is applicable to proteins of known structures. With rapidly increasing number of solved protein structures, the method has wide applicability in purification, targeting, and sensing of proteins.

  DOI：

  10.1021/ja003193z