[4-(3-isopropyl-4-methoxy-benzyl)-3,5-dimethyl-phenoxy]-acetic acid

• 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-methoxy-benzyl)-3,5-dimethyl-phenoxy]-acetic acid
• 英文别名: 2-[4-[(4-Methoxy-3-propan-2-ylphenyl)methyl]-3,5-dimethylphenoxy]acetic acid
• 化学式: C₂₁H₂₆O₄
• 分子量: 342.435
• InChiKey: SPTFRHOUYLOHMM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.2
• 重原子数：
  25
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  55.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  4-bromo-2-isopropylanisole 在 palladium on activated charcoal sodium hydroxide 、 正丁基锂 、 氢气 、 caesium carbonate 作用下， 以 四氢呋喃 、 甲醇 、 乙醇 、 溶剂黄146 、 N,N-二甲基甲酰胺 为溶剂， -78.0~20.0 ℃ 、101.33 kPa 条件下， 反应 18.0h， 生成 [4-(3-isopropyl-4-methoxy-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

文献信息

• A Functionally Orthogonal Ligand−Receptor Pair Created by Targeting the Allosteric Mechanism of the Thyroid Hormone Receptor
  作者：A. Quamrul Hassan、John T. Koh

  DOI：10.1021/ja060760v

  日期：2006.7.1

  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.