2-(4,4'-dibenzyloxybenzhydryl)benzyl cyanide | 530135-38-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: 2-(4,4'-dibenzyloxybenzhydryl)benzyl cyanide
• 英文别名: 2-[2-[bis(4-phenylmethoxyphenyl)methyl]phenyl]acetonitrile
• CAS: 530135-38-7
• 化学式: C₃₅H₂₉NO₂
• 分子量: 495.621
• InChiKey: IVKIMFZBCZPERT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.09
• 重原子数：
  38.0
• 可旋转键数：
  10.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  42.25
• 氢给体数：
  0.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  2-(4,4'-dibenzyloxybenzhydryl)benzyl cyanide 在 palladium on activated charcoal sodium hydroxide 、 氢气 作用下， 以 甲醇 为溶剂， 反应 15.0h， 生成 2-[2-[Bis(4-hydroxyphenyl)methyl]phenyl]acetamide
  参考文献：
  名称：

  Nitrophenyl Derivatives as Aldose Reductase Inhibitors

  摘要：

  Nitrophenyl derivatives ere recently discovered as a new class of ALR2 inhibitors by means of docking and database screening of the National Cancer Institute database of organic molecules. The nitro group was predicted to bind to the Tyr48 and His110 active site residues of the enzyme. the site adhere acidic ALR2 inhibitors such as carboxylic acids bind in their anionic form. Given the novelty of these Compounds. we decided to expand their structure-activity relationships by synthesizing and testing a series of derivatives and the corresponding compounds having a carboxylic group instead of the nitro moiety: the results obtained were rationalized by means of docking and molecular dynamics simulations. On the whole there is an agreement between inhibitory data and the results of molecular modeling experiments. supporting the hypothesized binding mode of these compounds. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(02)00318-8
• 作为产物：
  描述：

  methyl 2-(4,4'-dibenzyloxybenzhydryl)benzoate 在 lithium aluminium tetrahydride 、 三溴化磷 作用下， 以 乙醚 、 二氯甲烷 、 二甲基亚砜 为溶剂， 反应 5.0h， 生成 2-(4,4'-dibenzyloxybenzhydryl)benzyl cyanide
  参考文献：
  名称：

  Nitrophenyl Derivatives as Aldose Reductase Inhibitors

  摘要：

  Nitrophenyl derivatives ere recently discovered as a new class of ALR2 inhibitors by means of docking and database screening of the National Cancer Institute database of organic molecules. The nitro group was predicted to bind to the Tyr48 and His110 active site residues of the enzyme. the site adhere acidic ALR2 inhibitors such as carboxylic acids bind in their anionic form. Given the novelty of these Compounds. we decided to expand their structure-activity relationships by synthesizing and testing a series of derivatives and the corresponding compounds having a carboxylic group instead of the nitro moiety: the results obtained were rationalized by means of docking and molecular dynamics simulations. On the whole there is an agreement between inhibitory data and the results of molecular modeling experiments. supporting the hypothesized binding mode of these compounds. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(02)00318-8