tris(2,6-dicarboxylphenyl) trimesate

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 缩酚酸和缩酚酸环醚类
• 英文名称: tris(2,6-dicarboxylphenyl) trimesate
• 英文别名: 2-[3,5-Bis[(2,6-dicarboxyphenoxy)carbonyl]benzoyl]oxybenzene-1,3-dicarboxylic acid
• 化学式: C₃₃H₁₈O₁₈
• 分子量: 702.495
• InChiKey: GQDCRVHPSNPXCO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  51
• 可旋转键数：
  15
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  303
• 氢给体数：
  6
• 氢受体数：
  18

反应信息

• 作为产物：
  描述：

  1,3,5-苯三甲酰氯 在 potassium tert-butylate 、 三氟乙酸 作用下， 以 四氢呋喃 为溶剂， 反应 1.0h， 生成 tris(2,6-dicarboxylphenyl) trimesate
  参考文献：
  名称：

  Mechanism of Site-Directed Protein Cross-Linking. Protein-Directed Selectivity in Reactions of Hemoglobin with Aryl Trimesates

  摘要：

  Site-directed cross-linking of hemoglobin has become an efficient way to produce a structurally defined altered protein with desirable functional properties. The reagent trimesoyl tris(3,5-dibromosalicylate) (1) introduces a bis amide cross-link derived from the epsilon-amino groups of the side chains of the two beta-Lys-82 residues in human hemoglobin. The basis of its specificity was investigated using a set of analogues of 1 (2-12). There are marked differences in the reaction patterns of these compounds with amino groups in hemoglobin compared to reactions with n-propylamine. The compounds that effectively modify the protein contain a carboxyl group ortho to the phenolic oxygen of the ester, while materials with meta or para carboxyl groups give little or no reaction. In contrast, the reactions with n-propylamine are slowest with the ortho carboxyl materials. Addition of the unreactive compound 5 to a solution containing hemoglobin reduces the ability of 1 to modify the protein, showing that the unreactive compound binds but does not react. On the basis of these observations and the known reaction patterns of salicylates, it is clear that: the environment in the protein controls the reaction, regardless of the inherent reactivity of the reagent. We propose that the carboxyl group positions the reagent critically within the protein. Only the ortho arrangement permits transfer of the acyl function to the nucleophile.

  DOI：

  10.1021/jo991514n

文献信息

• Mechanism of Site-Directed Protein Cross-Linking. Protein-Directed Selectivity in Reactions of Hemoglobin with Aryl Trimesates
  作者：Ronald Kluger、Vittorio De Stefano

  DOI：10.1021/jo991514n

  日期：2000.1.1

  Site-directed cross-linking of hemoglobin has become an efficient way to produce a structurally defined altered protein with desirable functional properties. The reagent trimesoyl tris(3,5-dibromosalicylate) (1) introduces a bis amide cross-link derived from the epsilon-amino groups of the side chains of the two beta-Lys-82 residues in human hemoglobin. The basis of its specificity was investigated using a set of analogues of 1 (2-12). There are marked differences in the reaction patterns of these compounds with amino groups in hemoglobin compared to reactions with n-propylamine. The compounds that effectively modify the protein contain a carboxyl group ortho to the phenolic oxygen of the ester, while materials with meta or para carboxyl groups give little or no reaction. In contrast, the reactions with n-propylamine are slowest with the ortho carboxyl materials. Addition of the unreactive compound 5 to a solution containing hemoglobin reduces the ability of 1 to modify the protein, showing that the unreactive compound binds but does not react. On the basis of these observations and the known reaction patterns of salicylates, it is clear that: the environment in the protein controls the reaction, regardless of the inherent reactivity of the reagent. We propose that the carboxyl group positions the reagent critically within the protein. Only the ortho arrangement permits transfer of the acyl function to the nucleophile.