4,5,7-tribromobenzotriazole | 1240784-75-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并三唑类
• 英文名称: 4,5,7-tribromobenzotriazole
• 英文别名: 4,5,7-tribromo-2H-benzotriazole
• CAS: 1240784-75-1
• 化学式: C₆H₂Br₃N₃
• 分子量: 355.814
• InChiKey: XKFAZUZVANIUJF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  12
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  41.6
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  4,5,7-tribromobenzotriazole 在 硫酸 、 硝酸 作用下， 以69%的产率得到5-nitro-4,6,7-tribromo-1H-benzotriazole
  参考文献：
  名称：

  Relative Role of Halogen Bonds and Hydrophobic Interactions in Inhibition of Human Protein Kinase CK2α by Tetrabromobenzotriazole and Some C(5)-Substituted Analogues

  摘要：

  To examine the relative role of halogen bonding and hydrophobic interactions in the inhibition of human CK2 alpha by 4,5,6,7-tetrabromobenzotriazole (TBBt), we have synthesized a series of 5-substituted benzotriazoles (Bt) and the corresponding 5-substituted 4,6,7-tribromobenzotriazoles (Br(3)Bt) and examined their inhibition of human CK2 alpha relative to that of TBBt. The various C(5) substituents differ in size (H and CH3), electronegativity (NH2 and NO2), and hydrophobicity (COOH and Cl). Some substituents were halogen bond donors (Cl, Br), while others were fluorine bond donors (F and CF3). Most of the 5-substituted analogues of Br(3)Bt (with the exception of COOH and NH2) exhibited inhibitory activity comparable to that of TBBt, whereas the 5-substituted analogues of the parent Bt were only weakly active (Br, Cl, NO2, CF3) or inactive. The observed effect of the volume of a ligand molecule pointed to its predominant role in inhibitory activity, indicating that presumed halogen bonding, identified in crystal structures and by molecular modeling, is dominated by hydrophobic interactions. Extended QSAR analysis additionally pointed to the monoanion and a preference for the N(1)-H protomer of the neutral ligand as parameters crucial for prediction of inhibitory activity. This suggests that the monoanions of TBBt and its congeners are the active forms that efficiently bind to CK2 alpha, and the binding affinity is coupled with protomeric equilibrium of the neutral ligand.

  DOI：

  10.1021/jp102848y
• 作为产物：
  描述：

  5-carboxy-4,6,7-tribromo-1H-benzotriazole 在 喹啉 作用下， 反应 0.25h， 以68%的产率得到4,5,7-tribromobenzotriazole
  参考文献：
  名称：

  Relative Role of Halogen Bonds and Hydrophobic Interactions in Inhibition of Human Protein Kinase CK2α by Tetrabromobenzotriazole and Some C(5)-Substituted Analogues

  摘要：

  To examine the relative role of halogen bonding and hydrophobic interactions in the inhibition of human CK2 alpha by 4,5,6,7-tetrabromobenzotriazole (TBBt), we have synthesized a series of 5-substituted benzotriazoles (Bt) and the corresponding 5-substituted 4,6,7-tribromobenzotriazoles (Br(3)Bt) and examined their inhibition of human CK2 alpha relative to that of TBBt. The various C(5) substituents differ in size (H and CH3), electronegativity (NH2 and NO2), and hydrophobicity (COOH and Cl). Some substituents were halogen bond donors (Cl, Br), while others were fluorine bond donors (F and CF3). Most of the 5-substituted analogues of Br(3)Bt (with the exception of COOH and NH2) exhibited inhibitory activity comparable to that of TBBt, whereas the 5-substituted analogues of the parent Bt were only weakly active (Br, Cl, NO2, CF3) or inactive. The observed effect of the volume of a ligand molecule pointed to its predominant role in inhibitory activity, indicating that presumed halogen bonding, identified in crystal structures and by molecular modeling, is dominated by hydrophobic interactions. Extended QSAR analysis additionally pointed to the monoanion and a preference for the N(1)-H protomer of the neutral ligand as parameters crucial for prediction of inhibitory activity. This suggests that the monoanions of TBBt and its congeners are the active forms that efficiently bind to CK2 alpha, and the binding affinity is coupled with protomeric equilibrium of the neutral ligand.

  DOI：

  10.1021/jp102848y

文献信息

• Relative Role of Halogen Bonds and Hydrophobic Interactions in Inhibition of Human Protein Kinase CK2α by Tetrabromobenzotriazole and Some C(5)-Substituted Analogues
  作者：Romualda Wąsik、Maja Łebska、Krzysztof Felczak、Jarosław Poznański、David Shugar

  DOI：10.1021/jp102848y

  日期：2010.8.19

  To examine the relative role of halogen bonding and hydrophobic interactions in the inhibition of human CK2 alpha by 4,5,6,7-tetrabromobenzotriazole (TBBt), we have synthesized a series of 5-substituted benzotriazoles (Bt) and the corresponding 5-substituted 4,6,7-tribromobenzotriazoles (Br(3)Bt) and examined their inhibition of human CK2 alpha relative to that of TBBt. The various C(5) substituents differ in size (H and CH3), electronegativity (NH2 and NO2), and hydrophobicity (COOH and Cl). Some substituents were halogen bond donors (Cl, Br), while others were fluorine bond donors (F and CF3). Most of the 5-substituted analogues of Br(3)Bt (with the exception of COOH and NH2) exhibited inhibitory activity comparable to that of TBBt, whereas the 5-substituted analogues of the parent Bt were only weakly active (Br, Cl, NO2, CF3) or inactive. The observed effect of the volume of a ligand molecule pointed to its predominant role in inhibitory activity, indicating that presumed halogen bonding, identified in crystal structures and by molecular modeling, is dominated by hydrophobic interactions. Extended QSAR analysis additionally pointed to the monoanion and a preference for the N(1)-H protomer of the neutral ligand as parameters crucial for prediction of inhibitory activity. This suggests that the monoanions of TBBt and its congeners are the active forms that efficiently bind to CK2 alpha, and the binding affinity is coupled with protomeric equilibrium of the neutral ligand.