(E)-4-(3,5-bis(hexadecyloxy)styryl)phenol | 1338348-53-0

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 二苯乙烯类
• 英文名称: (E)-4-(3,5-bis(hexadecyloxy)styryl)phenol
• 英文别名: 4-[(E)-2-(3,5-dihexadecoxyphenyl)ethenyl]phenol
• CAS: 1338348-53-0
• 化学式: C₄₆H₇₆O₃
• 分子量: 677.108
• InChiKey: IHBSTLQFEMDSIK-QNEJGDQOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  19.3
• 重原子数：
  49
• 可旋转键数：
  34
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.7
• 拓扑面积：
  38.7
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  3,5-二羟基苯甲醇 在 四溴化碳 、 四丁基氟化铵 、 sodium hydride 、 potassium carbonate 、 三苯基膦 作用下， 以 四氢呋喃 、 二氯甲烷 、 丙酮 为溶剂， 反应 27.0h， 生成 (E)-4-(3,5-bis(hexadecyloxy)styryl)phenol
  参考文献：
  名称：

  Chemical modifications of resveratrol for improved protein kinase C alpha activity

  摘要：

  Resveratrol (1) is a naturally occurring phytoalexin that affects a variety of human disease models, including cardio-and neuroprotection, immune regulation, and cancer chemoprevention. One of the possible mechanisms by which resveratrol affects these disease states is by affecting the cellular signaling network involving protein kinase C alpha (PKC alpha). PKC alpha is a member of the family of serine/threonine kinases, whose activity is inhibited by resveratrol. To study the structure-activity relationship, several monoalkoxy, dialkoxy and hydroxy analogs of resveratrol have been synthesized, tested for their cytotoxic effects on HEK293 cells, measured their effects on the membrane translocation properties of PKC alpha in the presence and absence of the PKC activator TPA, and studied their binding with the activator binding domain of PKC alpha. The analogs showed less cytotoxic effects on HEK293 cells and caused higher membrane translocation (activation) than that of resveratrol. Among all the analogs, 3, 16 and 25 showed significantly higher activation than resveratrol. Resveratrol analogs, however, inhibited phorbol ester-induced membrane translocation, and the inhibition was less than that of resveratrol. Binding studies using steady state fluorescence spectroscopy indicated that resveratrol and the analogs bind to the second cysteine-rich domain of PKC alpha. The molecular docking studies indicated that resveratrol and the analogs interact with the protein by forming hydrogen bonds through its hydroxyl groups. These results signify that molecules developed on a resveratrol scaffold can attenuate PKC alpha activity and this strategy can be used to regulate various disease states involving PKC alpha. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.08.008

文献信息

• Chemical modifications of resveratrol for improved protein kinase C alpha activity
  作者：Joydip Das、Satyabrata Pany、Anjoy Majhi

  DOI：10.1016/j.bmc.2011.08.008

  日期：2011.9

  Resveratrol (1) is a naturally occurring phytoalexin that affects a variety of human disease models, including cardio-and neuroprotection, immune regulation, and cancer chemoprevention. One of the possible mechanisms by which resveratrol affects these disease states is by affecting the cellular signaling network involving protein kinase C alpha (PKC alpha). PKC alpha is a member of the family of serine/threonine kinases, whose activity is inhibited by resveratrol. To study the structure-activity relationship, several monoalkoxy, dialkoxy and hydroxy analogs of resveratrol have been synthesized, tested for their cytotoxic effects on HEK293 cells, measured their effects on the membrane translocation properties of PKC alpha in the presence and absence of the PKC activator TPA, and studied their binding with the activator binding domain of PKC alpha. The analogs showed less cytotoxic effects on HEK293 cells and caused higher membrane translocation (activation) than that of resveratrol. Among all the analogs, 3, 16 and 25 showed significantly higher activation than resveratrol. Resveratrol analogs, however, inhibited phorbol ester-induced membrane translocation, and the inhibition was less than that of resveratrol. Binding studies using steady state fluorescence spectroscopy indicated that resveratrol and the analogs bind to the second cysteine-rich domain of PKC alpha. The molecular docking studies indicated that resveratrol and the analogs interact with the protein by forming hydrogen bonds through its hydroxyl groups. These results signify that molecules developed on a resveratrol scaffold can attenuate PKC alpha activity and this strategy can be used to regulate various disease states involving PKC alpha. (C) 2011 Elsevier Ltd. All rights reserved.