(E)-methyl 2-(2-(6-(benzyloxy)-7-methoxy-3-oxo-3,4-dihydro-2H-benzo[b][1,4]oxazin-2-ylidene)ethyl)-3-chloro-4,6-dihydroxybenzoate | 1160152-75-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (E)-methyl 2-(2-(6-(benzyloxy)-7-methoxy-3-oxo-3,4-dihydro-2H-benzo[b][1,4]oxazin-2-ylidene)ethyl)-3-chloro-4,6-dihydroxybenzoate
• CAS: 1160152-75-9
• 化学式: C₂₆H₂₂ClNO₈
• 分子量: 511.916
• InChiKey: VXMGXMQTLMQZRO-DJKKODMXSA-N

物化性质

• 沸点：
  770.5±60.0 °C(predicted)
• 密度：
  1.449±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.58
• 重原子数：
  36.0
• 可旋转键数：
  7.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.15
• 拓扑面积：
  123.55
• 氢给体数：
  3.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  (E)-methyl 2-(2-(6-(benzyloxy)-7-methoxy-3-oxo-3,4-dihydro-2H-benzo[b][1,4]oxazin-2-ylidene)ethyl)-3-chloro-4,6-dihydroxybenzoate 在 aluminum (III) chloride 、 甲醇 作用下， 以 苯甲醚 为溶剂， 以83%的产率得到(E)-methyl 3-chloro-4,6-dihydroxy-2-(2-(6-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-benzo[b][1,4]oxazin-2-ylidene)ethyl)benzoate
  参考文献：
  名称：

  Design, Synthesis, and Biological Evaluation of Conformationally Constrained cis-Amide Hsp90 Inhibitors

  摘要：

  Conformationally constrained cis-amide chimeric inhibitors of Hsp90 have been synthesized and evaluated for their Hsp90 inhibitory activity. These new compounds exhibited Hsp90 ATPase inhibition and induced Hsp90-dependent client protein degradation in a dose-dependent manner. Biological data reported herein suggests that amide bond isomerization of geldanamycin derivatives plays an important role in affinity for the heteroprotein complex present in cancer cells.

  DOI：

  10.1021/ol900783m
• 作为产物：
  描述：

  在 四丁基氟化铵 作用下， 以 四氢呋喃 为溶剂， 以0.16 g的产率得到(E)-methyl 2-(2-(6-(benzyloxy)-7-methoxy-3-oxo-3,4-dihydro-2H-benzo[b][1,4]oxazin-2-ylidene)ethyl)-3-chloro-4,6-dihydroxybenzoate
  参考文献：
  名称：

  Design, Synthesis, and Biological Evaluation of Conformationally Constrained cis-Amide Hsp90 Inhibitors

  摘要：

  Conformationally constrained cis-amide chimeric inhibitors of Hsp90 have been synthesized and evaluated for their Hsp90 inhibitory activity. These new compounds exhibited Hsp90 ATPase inhibition and induced Hsp90-dependent client protein degradation in a dose-dependent manner. Biological data reported herein suggests that amide bond isomerization of geldanamycin derivatives plays an important role in affinity for the heteroprotein complex present in cancer cells.

  DOI：

  10.1021/ol900783m