2-amino-4-bromoindane-2-phosphonic acid

• 分子结构分类: 有机化合物 - 苯类化合物 - 茚满类
• 英文名称: 2-amino-4-bromoindane-2-phosphonic acid
• 英文别名: (2-Amino-4-bromo-1,3-dihydroinden-2-yl)phosphonic acid
• 化学式: C₉H₁₁BrNO₃P
• 分子量: 292.069
• InChiKey: UECADYGADXORPJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.2
• 重原子数：
  15
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  83.6
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  1-溴-2,3-双(溴甲基)苯 在 盐酸 、 sodium hydroxide 、 二苯基膦叠氮化物 、 四丁基溴化铵 、 水 、 三乙胺 作用下， 以 乙醇 、 甲苯 为溶剂， 反应 33.83h， 生成 2-amino-4-bromoindane-2-phosphonic acid
  参考文献：
  名称：

  Inhibitors of phenylalanine ammonia-lyase: Substituted derivatives of 2-aminoindane-2-phosphonic acid and 1-aminobenzylphosphonic acid

  摘要：

  Six derivatives of 2-aminoindane-2-phosphonic acid and 1-aminobenzylphosphonic acid were synthesized. The compounds were tested both as inhibitors of buckwheat phenylalanine ammonia-lyase (in vitro) and as inhibitors of anthocyanin biosynthesis (in vivo). (+/-)-2-Amino-4-bromoindane-2-phosphonic acid was found to be the strongest inhibitor from investigated compounds. The results obtained are a basis for design of phenylalanine ammonia-lyase inhibitors useful in the enzyme structure studies in photo labelling experiments. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.phytochem.2006.11.022

文献信息

• Inhibitors of phenylalanine ammonia-lyase: Substituted derivatives of 2-aminoindane-2-phosphonic acid and 1-aminobenzylphosphonic acid
  作者：Piotr Miziak、Jerzy Zoń、Nikolaus Amrhein、Roman Gancarz

  DOI：10.1016/j.phytochem.2006.11.022

  日期：2007.2

  Six derivatives of 2-aminoindane-2-phosphonic acid and 1-aminobenzylphosphonic acid were synthesized. The compounds were tested both as inhibitors of buckwheat phenylalanine ammonia-lyase (in vitro) and as inhibitors of anthocyanin biosynthesis (in vivo). (+/-)-2-Amino-4-bromoindane-2-phosphonic acid was found to be the strongest inhibitor from investigated compounds. The results obtained are a basis for design of phenylalanine ammonia-lyase inhibitors useful in the enzyme structure studies in photo labelling experiments. (c) 2006 Elsevier Ltd. All rights reserved.