4-carbonyl-trans-cinnamoyl bis(tert-butyl-3,5-dibromosalicylate) | 183893-20-1

• 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: 4-carbonyl-trans-cinnamoyl bis(tert-butyl-3,5-dibromosalicylate)
• 英文别名: tert-butyl 3,5-dibromo-2-[(E)-3-[4-[2,4-dibromo-6-[(2-methylpropan-2-yl)oxycarbonyl]phenoxy]carbonylphenyl]prop-2-enoyl]oxybenzoate
• CAS: 183893-20-1
• 化学式: C₃₂H₂₈Br₄O₈
• 分子量: 860.186
• InChiKey: FHWWNGAUDPACHJ-FMIVXFBMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.6
• 重原子数：
  44
• 可旋转键数：
  13
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  105
• 氢给体数：
  0
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  4-carbonyl-trans-cinnamoyl bis(tert-butyl-3,5-dibromosalicylate) 在 三氟乙酸 作用下， 反应 0.17h， 以84%的产率得到4-carbonyl-trans-cinnamoyl bis(3,5-dibromosalicylate)
  参考文献：
  名称：

  Systematically Cross-Linked Human Hemoglobin:  Functional Effects of 10 Å Spans between Beta Subunits at Lysine-82

  摘要：

  The structure and properties of hemoglobin are altered by the introduction of cross-links of defined structure between specific residues, The bis methyl phosphates and bis 3,5-dibromosalicylates of 4-carbuxy-trans-cinnamic acid as well as the bis methyl phosphate of 2,6-naphthalenedicarboxylic acid produce a 10 Angstrom cross-link between the epsilon-amino groups of each beta-lys-82 of human hemoglobin. The oxygen affinity of the modified proteins fits the correlation interpolated from those for shorter and longer cross-links. The oxygen binding curve shows a high degree of cooperativity. These results support the idea that the length of the semirigid cross-link in a structurally homogeneous series constrains the relaxation of the protein upon oxygen binding by a mechanism that is specifically reflected in the oxygen affinity, while interactions between hemes that affect cooperativity are not diminished.

  DOI：

  10.1021/ja961443z
• 作为产物：
  描述：

  trans-p-carboxycinnamic acid 在 草酰氯 、 potassium tert-butylate 、 N,N-二甲基甲酰胺 作用下， 以 二氯甲烷 为溶剂， 反应 4.25h， 生成 4-carbonyl-trans-cinnamoyl bis(tert-butyl-3,5-dibromosalicylate)
  参考文献：
  名称：

  Systematically Cross-Linked Human Hemoglobin:  Functional Effects of 10 Å Spans between Beta Subunits at Lysine-82

  摘要：

  The structure and properties of hemoglobin are altered by the introduction of cross-links of defined structure between specific residues, The bis methyl phosphates and bis 3,5-dibromosalicylates of 4-carbuxy-trans-cinnamic acid as well as the bis methyl phosphate of 2,6-naphthalenedicarboxylic acid produce a 10 Angstrom cross-link between the epsilon-amino groups of each beta-lys-82 of human hemoglobin. The oxygen affinity of the modified proteins fits the correlation interpolated from those for shorter and longer cross-links. The oxygen binding curve shows a high degree of cooperativity. These results support the idea that the length of the semirigid cross-link in a structurally homogeneous series constrains the relaxation of the protein upon oxygen binding by a mechanism that is specifically reflected in the oxygen affinity, while interactions between hemes that affect cooperativity are not diminished.

  DOI：

  10.1021/ja961443z

文献信息

• Systematically Cross-Linked Human Hemoglobin:  Functional Effects of 10 Å Spans between Beta Subunits at Lysine-82
  作者：Ronald Kluger、Lixin Shen、Hong Xiao、Richard T. Jones

  DOI：10.1021/ja961443z

  日期：1996.1.1

  The structure and properties of hemoglobin are altered by the introduction of cross-links of defined structure between specific residues, The bis methyl phosphates and bis 3,5-dibromosalicylates of 4-carbuxy-trans-cinnamic acid as well as the bis methyl phosphate of 2,6-naphthalenedicarboxylic acid produce a 10 Angstrom cross-link between the epsilon-amino groups of each beta-lys-82 of human hemoglobin. The oxygen affinity of the modified proteins fits the correlation interpolated from those for shorter and longer cross-links. The oxygen binding curve shows a high degree of cooperativity. These results support the idea that the length of the semirigid cross-link in a structurally homogeneous series constrains the relaxation of the protein upon oxygen binding by a mechanism that is specifically reflected in the oxygen affinity, while interactions between hemes that affect cooperativity are not diminished.