(1E,4Z,6E)-7-(4-(hexadecyloxy)-3-methoxyphenyl)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one | 1219710-94-7

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 二芳基庚烷
• 英文名称: (1E,4Z,6E)-7-(4-(hexadecyloxy)-3-methoxyphenyl)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
• 英文别名: (1E,4Z,6E)-7-(4-hexadecoxy-3-methoxyphenyl)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
• CAS: 1219710-94-7
• 化学式: C₃₇H₅₂O₆
• 分子量: 592.816
• InChiKey: WFJKRLNKTQSGOK-JRYGYSFXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  12.1
• 重原子数：
  43
• 可旋转键数：
  23
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.49
• 拓扑面积：
  85.2
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  姜黄素 、 溴代十六烷 在 potassium carbonate 作用下， 以 丙酮 为溶剂， 以49%的产率得到(1E,4Z,6E)-7-(4-(hexadecyloxy)-3-methoxyphenyl)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
  参考文献：
  名称：

  Binding of curcumin and its long chain derivatives to the activator binding domain of novel protein kinase C

  摘要：

  Protein kinase C (PKC) is a family of serine/threonine kinases that play a central role in cellular signal transduction. The second messenger diacylglycerol having two long carbon chains acts as the endogenous ligand for the PKCs. Polyphenol curcumin, the active constituent of Curcuma longa is an anti-cancer agent and modulates PKC activity. To develop curcumin derivatives as effective PKC activators, we synthesized several long chain derivatives of curcumin, characterized their absorption and fluorescence properties and studied their interaction with the activator binding second cysteine-rich C1B subdomain of PKC delta, PKC epsilon and PKC theta. Curcumin (1) and its C16 long chain analog (4) quenched the intrinsic fluorescence of PKC delta C1B, PKC epsilon C1B and PKC theta C1B in a manner similar to that of PKC activator 12-O-tetradecanoylphorbol 13-acetate (TPA). The EC(50)s of the curcumin derivatives for fluorescence quenching varied in the range of 4-11 mu M, whereas, EC(50)s for TPA varied in the range of 3-6 mu M. Fluorescence emission maxima of 1 and 4 were blue shifted and the fluorescence anisotropy values were increased in the presence of the C1B domains in a manner similar to that shown by the fluorescent analog of TPA, sapintoxin-D, confirming that they were bound to the proteins. Molecular docking of 1 and 4 with novel PKC C1B revealed that both the molecules form hydrogen bonds with the protein residues. The present result shows that curcumin and its long chain derivatives bind to the C1B subdomain of novel PKCs and can be further modified structurally to improve its binding and activity. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.12.075

文献信息

• Binding of curcumin and its long chain derivatives to the activator binding domain of novel protein kinase C
  作者：Anjoy Majhi、Ghazi M. Rahman、Shyam Panchal、Joydip Das

  DOI：10.1016/j.bmc.2009.12.075

  日期：2010.2

  Protein kinase C (PKC) is a family of serine/threonine kinases that play a central role in cellular signal transduction. The second messenger diacylglycerol having two long carbon chains acts as the endogenous ligand for the PKCs. Polyphenol curcumin, the active constituent of Curcuma longa is an anti-cancer agent and modulates PKC activity. To develop curcumin derivatives as effective PKC activators, we synthesized several long chain derivatives of curcumin, characterized their absorption and fluorescence properties and studied their interaction with the activator binding second cysteine-rich C1B subdomain of PKC delta, PKC epsilon and PKC theta. Curcumin (1) and its C16 long chain analog (4) quenched the intrinsic fluorescence of PKC delta C1B, PKC epsilon C1B and PKC theta C1B in a manner similar to that of PKC activator 12-O-tetradecanoylphorbol 13-acetate (TPA). The EC(50)s of the curcumin derivatives for fluorescence quenching varied in the range of 4-11 mu M, whereas, EC(50)s for TPA varied in the range of 3-6 mu M. Fluorescence emission maxima of 1 and 4 were blue shifted and the fluorescence anisotropy values were increased in the presence of the C1B domains in a manner similar to that shown by the fluorescent analog of TPA, sapintoxin-D, confirming that they were bound to the proteins. Molecular docking of 1 and 4 with novel PKC C1B revealed that both the molecules form hydrogen bonds with the protein residues. The present result shows that curcumin and its long chain derivatives bind to the C1B subdomain of novel PKCs and can be further modified structurally to improve its binding and activity. (C) 2010 Elsevier Ltd. All rights reserved.