[(2-{3,5-Bis-[2-(bis-ethoxycarbonylmethyl-amino)-ethylcarbamoyl]-benzoylamino}-ethyl)-ethoxycarbonylmethyl-amino]-acetic acid ethyl ester | 352689-22-6

• 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: [(2-{3,5-Bis-[2-(bis-ethoxycarbonylmethyl-amino)-ethylcarbamoyl]-benzoylamino}-ethyl)-ethoxycarbonylmethyl-amino]-acetic acid ethyl ester
• CAS: 352689-22-6
• 化学式: C₃₉H₆₀N₆O₁₅
• 分子量: 852.937
• InChiKey: NEUXHEHDNCQKFP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.84
• 重原子数：
  60.0
• 可旋转键数：
  30.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  254.82
• 氢给体数：
  3.0
• 氢受体数：
  18.0

反应信息

• 作为反应物：
  描述：

  [(2-{3,5-Bis-[2-(bis-ethoxycarbonylmethyl-amino)-ethylcarbamoyl]-benzoylamino}-ethyl)-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69%的产率得到[(2-{3,5-Bis-[2-(bis-carboxymethyl-amino)-ethylcarbamoyl]-benzoylamino}-ethyl)-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：

  均苯三甲酸 、 在 (benzotriazo-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate 、 三乙胺 作用下， 以 乙腈 为溶剂， 反应 24.0h， 以34%的产率得到[(2-{3,5-Bis-[2-(bis-ethoxycarbonylmethyl-amino)-ethylcarbamoyl]-benzoylamino}-ethyl)-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

文献信息

• Recognition of Flexible Peptides in Water by Transition Metal Complexes
  作者：Shuguang Sun、Md. Abul Fazal、Bidhan C. Roy、Sanku Mallik

  DOI：10.1021/ol005555d

  日期：2000.4.1

  [GRAPHICS]This paper describes the design, synthesis, and evaluation of transition metal complexes capable of recognizing flexible histidine-containing peptides in aqueous medium (25 mM HEPES buffer, pH = 7.0, 25 degrees C). When the pattern of metal ions on a complex matches with the pattern of histidine moieties on the peptide, strong interaction (K = 1.2 x 10(6) M-1) can be achieved. The complex was highly selective (>200:1) in discriminating similar flexible peptides differing only by one glycine unit.