2-(2,3,6-trimethoxyphenyl)ethanol | 913621-92-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: 2-(2,3,6-trimethoxyphenyl)ethanol
• CAS: 913621-92-8
• 化学式: C₁₁H₁₆O₄
• 分子量: 212.246
• InChiKey: COOODMJGHMJELO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  15
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  47.9
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-(2,3,6-trimethoxyphenyl)ethanol 在 palladium on activated charcoal sodium chlorite 、 sodium periodate 、 sodium dihydrogenphosphate 、 四氧化锇 、 2-甲基-2-丁烯 、 偶氮二甲酸二异丙酯 、 氢气 、 硝酸 、 溶剂黄146 、 三苯基膦 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 乙醇 、 水 、 叔丁醇 为溶剂， 反应 19.0h， 生成 3-(2-((3-amino-2,5,6-trimethoxyphenethyloxy)carbonyl)-6-chloro-3,5-dihydroxyphenyl)propanoic acid
  参考文献：
  名称：

  Design, Synthesis, and StructureActivity Relationships for Chimeric Inhibitors of Hsp90

  摘要：

  Inhibition of the 90 kDa heat shock protein (Hsp90) family of molecular chaperones represents a promising new chemotherapeutic approach toward the treatment of several cancers. Previous studies have demonstrated that the natural products, radicicol and geldanamycin, are potent inhibitors of the Hsp90 N-terminal ATP binding site. The cocrystal structures of these molecules bound to Hsp90 have been determined, and through molecular modeling and superimposition of these ligands, hybrids of radicicol and geldanamycin have been designed. A series of macrocylic chimeras of radicicol and geldanamycin and the corresponding seco-agents have been prepared and evaluated for both antiproliferative activity and their ability to induce Hsp90-dependent client protein degradation.

  DOI：

  10.1021/jo061054f
• 作为产物：
  描述：

  环氧乙烷 、 1,2,4-三甲氧基苯 在 正丁基锂 作用下， 以 乙醚 为溶剂， 反应 4.0h， 以81%的产率得到2-(2,3,6-trimethoxyphenyl)ethanol
  参考文献：
  名称：

  Design, Synthesis, and StructureActivity Relationships for Chimeric Inhibitors of Hsp90

  摘要：

  Inhibition of the 90 kDa heat shock protein (Hsp90) family of molecular chaperones represents a promising new chemotherapeutic approach toward the treatment of several cancers. Previous studies have demonstrated that the natural products, radicicol and geldanamycin, are potent inhibitors of the Hsp90 N-terminal ATP binding site. The cocrystal structures of these molecules bound to Hsp90 have been determined, and through molecular modeling and superimposition of these ligands, hybrids of radicicol and geldanamycin have been designed. A series of macrocylic chimeras of radicicol and geldanamycin and the corresponding seco-agents have been prepared and evaluated for both antiproliferative activity and their ability to induce Hsp90-dependent client protein degradation.

  DOI：

  10.1021/jo061054f

文献信息

• Heat shock protein 90 inhibitors
  申请人：Blagg Brian

  公开号：US20070197787A1

  公开（公告）日：2007-08-23

  Novel compounds useful for inhibiting the 90 kDa heat shock proteins containing a quinone-like moiety and a di-hydroxy phenol like moiety, similar to geldanamycin and radicicol.
• HEAT SHOCK PROTEIN 90 INHIBITORS
  申请人：Blagg Brian S.J.

  公开号：US20100099865A1

  公开（公告）日：2010-04-22

  Novel compounds useful for inhibiting the 90kDa heat shock proteins containing a quinone-like moiety and a di-hydroxy phenol like moiety, similar to geldanamycin and radicicol.
• US7605288B2
  申请人：——

  公开号：US7605288B2

  公开（公告）日：2009-10-20
• US8188306B2
  申请人：——

  公开号：US8188306B2

  公开（公告）日：2012-05-29
• Design, Synthesis, and StructureActivity Relationships for Chimeric Inhibitors of Hsp90
  作者：Gang Shen、Mingwen Wang、Timothy R. Welch、Brian S. J. Blagg

  DOI：10.1021/jo061054f

  日期：2006.9.1

  Inhibition of the 90 kDa heat shock protein (Hsp90) family of molecular chaperones represents a promising new chemotherapeutic approach toward the treatment of several cancers. Previous studies have demonstrated that the natural products, radicicol and geldanamycin, are potent inhibitors of the Hsp90 N-terminal ATP binding site. The cocrystal structures of these molecules bound to Hsp90 have been determined, and through molecular modeling and superimposition of these ligands, hybrids of radicicol and geldanamycin have been designed. A series of macrocylic chimeras of radicicol and geldanamycin and the corresponding seco-agents have been prepared and evaluated for both antiproliferative activity and their ability to induce Hsp90-dependent client protein degradation.