4-(3-isopropyl-4-propoxy-benzyl)-3,5-dimethyl-phenol | 904925-62-8

• 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: 4-(3-isopropyl-4-propoxy-benzyl)-3,5-dimethyl-phenol
• CAS: 904925-62-8
• 化学式: C₂₁H₂₈O₂
• 分子量: 312.452
• InChiKey: HKDWVIMYXFBUAC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.51
• 重原子数：
  23.0
• 可旋转键数：
  6.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  29.46
• 氢给体数：
  1.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  4-(3-isopropyl-4-propoxy-benzyl)-3,5-dimethyl-phenol 在 sodium hydroxide 、 caesium carbonate 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 3.5h， 生成 [4-(3-isopropyl-4-propoxy-benzyl)-3,5-dimethyl-phenoxy]-acetic acid
  参考文献：
  名称：

  A Functionally Orthogonal Ligand−Receptor Pair Created by Targeting the Allosteric Mechanism of the Thyroid Hormone Receptor

  摘要：

  Nuclear receptors are ligand-dependent transcription factors that are of interest as potential tools to artificially regulate gene expression. Ligand binding induces a conformational change involving helix-12 which forms part of the dimerization interface used to bind transcriptional coactivators. When triiodothyronine (T3) binds the thyroid hormone receptor (TR) it indirectly contacts helix-12 through intermediary residues His(435) and Phe(451) termed a His-Phe switch. The mutant TR beta(H435A) is nonresponsive to physiological concentrations of T3 but can be activated by the synthetic hormone analogue QH2 which potently activates His435 -> Ala mutant at concentrations that do not activate the wild-type receptors TR alpha and TR beta. QH2 does not show antagonist behavior with the wild-type TRs. QH2's functionally orthogonal behavior with TR beta(H435A) is preserved on the three consensus thyroid hormone response elements.

  DOI：

  10.1021/ja060760v
• 作为产物：
  描述：

  4-苄氧基-2,6-二甲基苯甲醛 在 palladium on activated charcoal 正丁基锂 、 氢气 作用下， 以 四氢呋喃 、 乙醇 、 溶剂黄146 为溶剂， -78.0~20.0 ℃ 、101.33 kPa 条件下， 反应 14.5h， 生成 4-(3-isopropyl-4-propoxy-benzyl)-3,5-dimethyl-phenol
  参考文献：
  名称：

  A Functionally Orthogonal Ligand−Receptor Pair Created by Targeting the Allosteric Mechanism of the Thyroid Hormone Receptor

  摘要：

  Nuclear receptors are ligand-dependent transcription factors that are of interest as potential tools to artificially regulate gene expression. Ligand binding induces a conformational change involving helix-12 which forms part of the dimerization interface used to bind transcriptional coactivators. When triiodothyronine (T3) binds the thyroid hormone receptor (TR) it indirectly contacts helix-12 through intermediary residues His(435) and Phe(451) termed a His-Phe switch. The mutant TR beta(H435A) is nonresponsive to physiological concentrations of T3 but can be activated by the synthetic hormone analogue QH2 which potently activates His435 -> Ala mutant at concentrations that do not activate the wild-type receptors TR alpha and TR beta. QH2 does not show antagonist behavior with the wild-type TRs. QH2's functionally orthogonal behavior with TR beta(H435A) is preserved on the three consensus thyroid hormone response elements.

  DOI：

  10.1021/ja060760v