N-para-methoxybenzyl-N-(2-bromoacetyl)-O-methyltyrosine methyl ester

• 分子结构分类: 有机化合物 - 生物碱及其衍生物 - 石蒜科生物碱
• 英文名称: N-para-methoxybenzyl-N-(2-bromoacetyl)-O-methyltyrosine methyl ester
• 英文别名: methyl (2S)-2-[(2-bromoacetyl)-[(4-methoxyphenyl)methyl]amino]-3-(4-methoxyphenyl)propanoate
• 化学式: C₂₁H₂₄BrNO₅
• 分子量: 450.329
• InChiKey: KCWGRHCCUICQCS-IBGZPJMESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  28
• 可旋转键数：
  10
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  65.1
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-para-methoxybenzyl-N-(2-bromoacetyl)-O-methyltyrosine methyl ester 在 氨 作用下， 以 甲醇 为溶剂， 反应 48.0h， 以89%的产率得到N-para-methoxybenzyl-6-(para-methoxybenzyl)piperazine-2,5-dione
  参考文献：
  名称：

  Design, synthesis, and characterization of piperazinedione-based dual protein inhibitors for both farnesyltransferase and geranylgeranyltransferase-I

  摘要：

  Farnesyltransferase (FTase) and geranylgeranyltransferase type-I (GGTase-I) both catalyze the prenylation of protein substrate containing a typical -CAAX motif at the carboxyl terminus. The inhibitors for these two enzymes have been widely studied as potential cancer chemotherapeutic agents. In the present study, various piperazinedione derivatives were designed and synthesized as a new type of peptide mimetic compounds, which were characterized and found to be dual protein inhibitors for both FTase and GGTase-l. These compounds have similar chemical and physical properties to -CAAX motif of the protein substrate, which may facilitate their transfer to appropriate drug target in vivo. The best inhibitor compound 26b was found to occupy both isoprenoid and peptide substrate binding sites through kinetics and computer molecular docking studies. (C) 2011 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2011.03.007
• 作为产物：
  描述：

  4-甲氧基苯甲醛 在 sodium tetrahydroborate 、 三乙胺 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 9.0h， 生成 N-para-methoxybenzyl-N-(2-bromoacetyl)-O-methyltyrosine methyl ester
  参考文献：
  名称：

  Design, synthesis, and characterization of piperazinedione-based dual protein inhibitors for both farnesyltransferase and geranylgeranyltransferase-I

  摘要：

  Farnesyltransferase (FTase) and geranylgeranyltransferase type-I (GGTase-I) both catalyze the prenylation of protein substrate containing a typical -CAAX motif at the carboxyl terminus. The inhibitors for these two enzymes have been widely studied as potential cancer chemotherapeutic agents. In the present study, various piperazinedione derivatives were designed and synthesized as a new type of peptide mimetic compounds, which were characterized and found to be dual protein inhibitors for both FTase and GGTase-l. These compounds have similar chemical and physical properties to -CAAX motif of the protein substrate, which may facilitate their transfer to appropriate drug target in vivo. The best inhibitor compound 26b was found to occupy both isoprenoid and peptide substrate binding sites through kinetics and computer molecular docking studies. (C) 2011 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2011.03.007