methyl 6-[4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]phenoxy]hexanoate | 1043627-71-9

• 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: methyl 6-[4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]phenoxy]hexanoate
• CAS: 1043627-71-9
• 化学式: C₂₁H₂₄O₅
• 分子量: 356.419
• InChiKey: RIUVVQHRQBXJAX-VOTSOKGWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.3
• 重原子数：
  26
• 可旋转键数：
  10
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  76
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  methyl 6-[4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]phenoxy]hexanoate 在 氢氧化钾 作用下， 以 甲醇 为溶剂， 反应 24.0h， 以62%的产率得到Resveratrol Hexanoic Acid
  参考文献：
  名称：

  Design, synthesis and spectroscopic studies of resveratrol aliphatic acid ligands of human serum albumin

  摘要：

  As one of the natural polyphenols, resveratrol possesses hydroxyl substituted trans-stilbene structure and exerts impact on health by inhibiting multiple human enzymes, such as cyclooxygenase, F1 ATPase, and tyrosinase. Resveratrol has to be bound by human serum albumin (HSA) to keep a high concentration in serum, since its solubility is low in water. To improve water solubility and bioavailability, two resveratrol aliphatic acids and their esters have been designed and synthesized. The solubilities of the resveratrol and its derivatives have been measured using a standard procedure. The two aliphatic acids showed better solubilities in pure water and phosphate buffer (pH 7). The binding affinities of resveratrol derivatives for HSA were also measured, and the drug -protein interaction mechanism was investigated using fluorescence, UV -vis, and NMR spectroscopies. Interestingly, resveratrol hexanoic acid (5) was found to be a much better ligand (K(a) = (6.70 +/- 0.10) x 106 M (1)) for HSA than resveratrol (Ka = (1.64 +/- 0.07) x 105 M (1)), and there was 41-fold improvement for the binding affinity. It was the first time that the increase of fluorescence of resveratrol moiety was observed during the binding to HSA, suggesting that 5 should be bound tightly by HSA. The UV -vis absorption spectroscopy revealed a maximum absorption shift from 318 to 311 nm with decreasing intensity by 20% upon complexation, suggesting that the p -p conjugation of the stilbene structure was impaired during the binding. Although HSA was reported to have only one binding site for resveratrol, the Job's and molar ratio plots suggested that HSA should bind two molecules of 5. NMR study suggested that phenyl group (B ring) in the center of the molecule of 5 should be involved in the p -p stacking interactions with HSA aromatic amino acid residues. Molecular geometry calculation of 5 with Spartan software showed that the stilbene structure had two conformers, orthogonal and planar ones. The former (E = -1.432 KJ/mol) was more stable than the latter (E = -0.128 KJ/mol), suggesting that the former should be the conformer of 5 in the complexation with HSA. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.05.002
• 作为产物：
  描述：

  6-溴己酸甲酯 、 白藜芦醇 在 potassium carbonate 作用下， 以 丙酮 为溶剂， 反应 16.0h， 以9%的产率得到methyl 6-[4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]phenoxy]hexanoate
  参考文献：
  名称：

  Design, synthesis and spectroscopic studies of resveratrol aliphatic acid ligands of human serum albumin

  摘要：

  As one of the natural polyphenols, resveratrol possesses hydroxyl substituted trans-stilbene structure and exerts impact on health by inhibiting multiple human enzymes, such as cyclooxygenase, F1 ATPase, and tyrosinase. Resveratrol has to be bound by human serum albumin (HSA) to keep a high concentration in serum, since its solubility is low in water. To improve water solubility and bioavailability, two resveratrol aliphatic acids and their esters have been designed and synthesized. The solubilities of the resveratrol and its derivatives have been measured using a standard procedure. The two aliphatic acids showed better solubilities in pure water and phosphate buffer (pH 7). The binding affinities of resveratrol derivatives for HSA were also measured, and the drug -protein interaction mechanism was investigated using fluorescence, UV -vis, and NMR spectroscopies. Interestingly, resveratrol hexanoic acid (5) was found to be a much better ligand (K(a) = (6.70 +/- 0.10) x 106 M (1)) for HSA than resveratrol (Ka = (1.64 +/- 0.07) x 105 M (1)), and there was 41-fold improvement for the binding affinity. It was the first time that the increase of fluorescence of resveratrol moiety was observed during the binding to HSA, suggesting that 5 should be bound tightly by HSA. The UV -vis absorption spectroscopy revealed a maximum absorption shift from 318 to 311 nm with decreasing intensity by 20% upon complexation, suggesting that the p -p conjugation of the stilbene structure was impaired during the binding. Although HSA was reported to have only one binding site for resveratrol, the Job's and molar ratio plots suggested that HSA should bind two molecules of 5. NMR study suggested that phenyl group (B ring) in the center of the molecule of 5 should be involved in the p -p stacking interactions with HSA aromatic amino acid residues. Molecular geometry calculation of 5 with Spartan software showed that the stilbene structure had two conformers, orthogonal and planar ones. The former (E = -1.432 KJ/mol) was more stable than the latter (E = -0.128 KJ/mol), suggesting that the former should be the conformer of 5 in the complexation with HSA. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.05.002

文献信息

• Design, synthesis and spectroscopic studies of resveratrol aliphatic acid ligands of human serum albumin
  作者：Yu Lin Jiang

  DOI：10.1016/j.bmc.2008.05.002

  日期：2008.6

  As one of the natural polyphenols, resveratrol possesses hydroxyl substituted trans-stilbene structure and exerts impact on health by inhibiting multiple human enzymes, such as cyclooxygenase, F1 ATPase, and tyrosinase. Resveratrol has to be bound by human serum albumin (HSA) to keep a high concentration in serum, since its solubility is low in water. To improve water solubility and bioavailability, two resveratrol aliphatic acids and their esters have been designed and synthesized. The solubilities of the resveratrol and its derivatives have been measured using a standard procedure. The two aliphatic acids showed better solubilities in pure water and phosphate buffer (pH 7). The binding affinities of resveratrol derivatives for HSA were also measured, and the drug -protein interaction mechanism was investigated using fluorescence, UV -vis, and NMR spectroscopies. Interestingly, resveratrol hexanoic acid (5) was found to be a much better ligand (K(a) = (6.70 +/- 0.10) x 106 M (1)) for HSA than resveratrol (Ka = (1.64 +/- 0.07) x 105 M (1)), and there was 41-fold improvement for the binding affinity. It was the first time that the increase of fluorescence of resveratrol moiety was observed during the binding to HSA, suggesting that 5 should be bound tightly by HSA. The UV -vis absorption spectroscopy revealed a maximum absorption shift from 318 to 311 nm with decreasing intensity by 20% upon complexation, suggesting that the p -p conjugation of the stilbene structure was impaired during the binding. Although HSA was reported to have only one binding site for resveratrol, the Job's and molar ratio plots suggested that HSA should bind two molecules of 5. NMR study suggested that phenyl group (B ring) in the center of the molecule of 5 should be involved in the p -p stacking interactions with HSA aromatic amino acid residues. Molecular geometry calculation of 5 with Spartan software showed that the stilbene structure had two conformers, orthogonal and planar ones. The former (E = -1.432 KJ/mol) was more stable than the latter (E = -0.128 KJ/mol), suggesting that the former should be the conformer of 5 in the complexation with HSA. (c) 2008 Elsevier Ltd. All rights reserved.