4-[6-(4-Bromophenyl)-5-ethoxycarbonyl-4-methyl-2-oxo-1,6-dihydropyrimidin-3-yl]butanoic acid | 831217-44-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: 4-[6-(4-Bromophenyl)-5-ethoxycarbonyl-4-methyl-2-oxo-1,6-dihydropyrimidin-3-yl]butanoic acid
• CAS: 831217-44-8
• 化学式: C₁₈H₂₁BrN₂O₅
• 分子量: 425.279
• InChiKey: IODPYTVEPBOYMC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  26
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  95.9
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  4-脲基丁酸 、 乙酰乙酸乙酯 、 对溴苯甲醛 在 盐酸 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.67h， 生成 4-[6-(4-Bromophenyl)-5-ethoxycarbonyl-4-methyl-2-oxo-1,6-dihydropyrimidin-3-yl]butanoic acid
  参考文献：
  名称：

  Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase

  摘要：

  Molecular chaperones, such as Hsp70 and Hsp90, are responsible for a variety of protective, anti-apoptotic functions. While inhibitors of Hsp90, such as geldanamycin and its derivative 17-AAG, are well known and important anti-cancer leads, Hsp70 has received less attention. Interesting lead candidates for Hsp70 share a dihydropyrimidine core; however, the preferred display of pendant functionality is still not clear. Here, we take advantage of the versatility of peptides to explore the requirements for activity. An exploratory compound collection was assembled by performing a Biginelli cyclocondensation at the terminus of a resin-bound beta-peptide. Liberation from solid support yielded peptide-modified dihydropyrimidines and, within this series, we uncovered compounds that alter the ATPase activity of Hsp70 and its bacterial ortholog, DnaK. Moreover, we identified important contributions made by aromatic, hydrophobic groups. These chemical probes could be used to study the roles of this molecular chaperone in disease. (C) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2007.11.027

文献信息

• Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase
  作者：Susanne Wisén、John Androsavich、Christopher G. Evans、Lyra Chang、Jason E. Gestwicki

  DOI：10.1016/j.bmcl.2007.11.027

  日期：2008.1

  Molecular chaperones, such as Hsp70 and Hsp90, are responsible for a variety of protective, anti-apoptotic functions. While inhibitors of Hsp90, such as geldanamycin and its derivative 17-AAG, are well known and important anti-cancer leads, Hsp70 has received less attention. Interesting lead candidates for Hsp70 share a dihydropyrimidine core; however, the preferred display of pendant functionality is still not clear. Here, we take advantage of the versatility of peptides to explore the requirements for activity. An exploratory compound collection was assembled by performing a Biginelli cyclocondensation at the terminus of a resin-bound beta-peptide. Liberation from solid support yielded peptide-modified dihydropyrimidines and, within this series, we uncovered compounds that alter the ATPase activity of Hsp70 and its bacterial ortholog, DnaK. Moreover, we identified important contributions made by aromatic, hydrophobic groups. These chemical probes could be used to study the roles of this molecular chaperone in disease. (C) 2007 Elsevier Ltd. All rights reserved.