[3-[[4-(Bromomethyl)-5-(cyanomethoxy)-2-phenylmethoxyphenyl]methyl]-4-(cyanomethoxy)phenyl] benzoate | 195601-76-4

• 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: [3-[[4-(Bromomethyl)-5-(cyanomethoxy)-2-phenylmethoxyphenyl]methyl]-4-(cyanomethoxy)phenyl] benzoate
• CAS: 195601-76-4
• 化学式: C₃₂H₂₅BrN₂O₅
• 分子量: 597.465
• InChiKey: WKWLITJAGFGSFS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.8
• 重原子数：
  40
• 可旋转键数：
  13
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.16
• 拓扑面积：
  102
• 氢给体数：
  0
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  [3-[[4-(Bromomethyl)-5-(cyanomethoxy)-2-phenylmethoxyphenyl]methyl]-4-(cyanomethoxy)phenyl] benzoate 在 氢氧化钾 、 四(三苯基膦)钯 、 1,2-二溴乙烷 、 锌 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 2.75h， 生成 (2-{2-Benzyloxy-4-[2-benzyloxy-4-(2-benzyloxy-5-carboxymethoxy-4-hydroxymethyl-benzyl)-5-carboxymethoxy-benzyl]-5-carboxymethoxy-benzyl}-4-hydroxy-phenoxy)-acetic acid
  参考文献：
  名称：

  Anionic- and Lipophilic-Mediated Surface Binding Inhibitors of Human Leukocyte Elastase

  摘要：

  We report the synthesis of a series of diphenylmethane-based oligomers containing anionic and lipophilic functionalities that are potent inhibitors of human leukocyte elastase (HLE). The enzyme inhibition is regulated by the size of the oligomer, as well as, the number of charges. Lipophilicity is an important element in determining potency and specificity against other basic enzymes. Compounds whose scaffolds contain three phenoxyacetic acid groups and three alkyl ethers are competitive and specific inhibitors of HLE with K-i 20 nM. The mechanism of action of this class of compounds is believed to involve multidendate interactions with the surface of HLE near the active site which prevents substrate access to the catalytic site.

  DOI：

  10.1021/jm970251r
• 作为产物：
  描述：

  2,5-二羟基苯甲醛 在 吗啉 、 咪唑 、 甲醇 、 4-二甲氨基吡啶 、 N,N-二甲基丙烯基脲 、 sodium tetrahydroborate 、 N-溴代丁二酰亚胺(NBS) 、 四(三苯基膦)钯 、 四丁基氟化铵 、 碘 、 sodium methylate 、 sodium hydride 、 potassium carbonate 、 溶剂黄146 、 1,2-二溴乙烷 、 三乙胺 、 三苯基膦 、 锌 作用下， 以 四氢呋喃 、 二氯甲烷 、 二乙二醇二甲醚 、 乙腈 为溶剂， 反应 29.17h， 生成 [3-[[4-(Bromomethyl)-5-(cyanomethoxy)-2-phenylmethoxyphenyl]methyl]-4-(cyanomethoxy)phenyl] benzoate
  参考文献：
  名称：

  Anionic- and Lipophilic-Mediated Surface Binding Inhibitors of Human Leukocyte Elastase

  摘要：

  We report the synthesis of a series of diphenylmethane-based oligomers containing anionic and lipophilic functionalities that are potent inhibitors of human leukocyte elastase (HLE). The enzyme inhibition is regulated by the size of the oligomer, as well as, the number of charges. Lipophilicity is an important element in determining potency and specificity against other basic enzymes. Compounds whose scaffolds contain three phenoxyacetic acid groups and three alkyl ethers are competitive and specific inhibitors of HLE with K-i 20 nM. The mechanism of action of this class of compounds is believed to involve multidendate interactions with the surface of HLE near the active site which prevents substrate access to the catalytic site.

  DOI：

  10.1021/jm970251r

文献信息

• Anionic- and Lipophilic-Mediated Surface Binding Inhibitors of Human Leukocyte Elastase
  作者：John Regan、Daniel McGarry、Joseph Bruno、Daniel Green、Jack Newman、Chin-Yi Hsu、Jane Kline、Jeffrey Barton、Jeffrey Travis、Yong Mi Choi、Francis Volz、Henry Pauls、Richard Harrison、Asher Zilberstein、Shmuel A. Ben-Sasson、Michael Chang

  DOI：10.1021/jm970251r

  日期：1997.10.1

  We report the synthesis of a series of diphenylmethane-based oligomers containing anionic and lipophilic functionalities that are potent inhibitors of human leukocyte elastase (HLE). The enzyme inhibition is regulated by the size of the oligomer, as well as, the number of charges. Lipophilicity is an important element in determining potency and specificity against other basic enzymes. Compounds whose scaffolds contain three phenoxyacetic acid groups and three alkyl ethers are competitive and specific inhibitors of HLE with K-i 20 nM. The mechanism of action of this class of compounds is believed to involve multidendate interactions with the surface of HLE near the active site which prevents substrate access to the catalytic site.