3,4-O-dicaffeoyl-1,5-γ-quinide

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 肉桂酸及其衍生物
• 英文名称: 3,4-O-dicaffeoyl-1,5-γ-quinide
• 英文别名: 3,4-dicaffeoyl-1,5-quinide
• 化学式: C₂₅H₂₂O₁₁
• 分子量: 498.443
• InChiKey: ZLYIWYCHNAZAQI-BBLPPJRLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.51
• 重原子数：
  36.0
• 可旋转键数：
  6.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.24
• 拓扑面积：
  180.05
• 氢给体数：
  5.0
• 氢受体数：
  11.0

反应信息

• 作为产物：
  描述：

  咖啡酸 在 吡啶 、 4-二甲氨基吡啶 、 氯化亚砜 、 三乙胺 、 lithium chloride 、 sodium hydroxide 作用下， 以 二氯甲烷 、 水 为溶剂， 反应 197.0h， 生成 3,4-O-dicaffeoyl-1,5-γ-quinide
  参考文献：
  名称：

  Interaction of chlorogenic acids and quinides from coffee with human serum albumin

  摘要：

  Chlorogenic acids and their derivatives are abundant in coffee and their composition changes between coffee species. Human serum albumin (HSA) interacts with this family of compounds with high affinity. We have studied by fluorescence spectroscopy the specific binding of HSA with eight compounds that belong to the coffee polyphenols family, four acids (caffeic acid, ferulic acid, 5-O-caffeoyl quinic acid, and 3,4-dimethoxycinnamic acid) and four lactones (3,4-O-dicaffeoyl-1,5-gamma-quinide, 3-O-[3,4-(dimethoxy)cinnamoyl]-1,5-gamma-quinide, 3,4-O-bis[3,4-(dimethoxy)cinnamoyl]-1,5-gamma-quinide, and 1,3, 4-O-tris[3,4-(dimethoxy)cinnamoyl]-1,5-gamma-quinide), finding dissociation constants of the albumin-chlorogenic acids and albumin-quinides complexes in the micromolar range, between 2 and 30 mu M. Such values are comparable with those of the most powerful binders of albumin, and more favourable than the values obtained for the majority of drugs. Interestingly in the case of 3,4-O-dicaffeoy1-1,5-gamma-quinide, we have observed the entrance of two ligand molecules in the same binding site, leading up to a first dissociation constant even in the hundred nanomolar range, which is to our knowledge the highest affinity ever observed for HSA and its ligands. The displacement of warfarin, a reference drug binding to HSA, by the quinide has also been demonstrated. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.foodchem.2014.07.080

文献信息

• Dicinnamoylquinides in roasted coffee inhibit the human adenosine transporter
  作者：Tomas de Paulis、Dennis E Schmidt、Aleksandra K Bruchey、Michael T Kirby、Michael P McDonald、Patricia Commers、David M Lovinger、Peter R Martin

  DOI：10.1016/s0014-2999(02)01540-6

  日期：2002.5

  Preliminary screening of a minor. non-xanthine constituent of roasted coffee, 3,4-diferuloyl-1,5-quinolactone (DIFEQ), showed inhibition of the adenosine transporter at low micromolar concentration. DIFEQ is a neutral derivative of the chlorogenic acids, i.e. isomeric mono- and di-substituted coumaroyl-, caffeoyl-, and feruloyl-esters of quinic acid, formed in the roasting process of coffee. Displacement of the adenosine transporter antagonist [H-3](S)-(nitrobenzyl)-6-thioinosine binding by DIFEQ in cultured U-937 cell preparations, expressing the human adenosine transporter protein (hENT1), showed a K-i of 0.96 +/- 0.13 muM. Extracts of regular and decaffeinated coffee showed binding activities equivalent to 30-40 mg DIFEQ per three cups of coffee. Acute administration of a high dose of DIFEQ (100 mg/kg i.p.) reduced open field locomotion in mice for 20 min in correlation with brain levels of DIFEQ Both 3,4-dicaffeoyl-1,5-quinide and 3,4-dicoumaroyl-1,5-quinide, two close structural analogs of DIFEQ also present in roasted coffee, showed similar affinities for the adenosine transporter, while the corresponding 3- and 4-mono caffeoyl- and feruloyl-quinides were one to two orders of magnitudes less active. This suggests that 3,4-dicinnamoyl-1,5-quinides in coffee could have the potential to raise extra-cellular adenosine levels, thereby counteracting the stimulant effect of caffeine. (C) 2002 Published by Elsevier Science B.V.
• Interaction of chlorogenic acids and quinides from coffee with human serum albumin
  作者：Valentina Sinisi、Cristina Forzato、Nicola Cefarin、Luciano Navarini、Federico Berti

  DOI：10.1016/j.foodchem.2014.07.080

  日期：2015.2

  Chlorogenic acids and their derivatives are abundant in coffee and their composition changes between coffee species. Human serum albumin (HSA) interacts with this family of compounds with high affinity. We have studied by fluorescence spectroscopy the specific binding of HSA with eight compounds that belong to the coffee polyphenols family, four acids (caffeic acid, ferulic acid, 5-O-caffeoyl quinic acid, and 3,4-dimethoxycinnamic acid) and four lactones (3,4-O-dicaffeoyl-1,5-gamma-quinide, 3-O-[3,4-(dimethoxy)cinnamoyl]-1,5-gamma-quinide, 3,4-O-bis[3,4-(dimethoxy)cinnamoyl]-1,5-gamma-quinide, and 1,3, 4-O-tris[3,4-(dimethoxy)cinnamoyl]-1,5-gamma-quinide), finding dissociation constants of the albumin-chlorogenic acids and albumin-quinides complexes in the micromolar range, between 2 and 30 mu M. Such values are comparable with those of the most powerful binders of albumin, and more favourable than the values obtained for the majority of drugs. Interestingly in the case of 3,4-O-dicaffeoy1-1,5-gamma-quinide, we have observed the entrance of two ligand molecules in the same binding site, leading up to a first dissociation constant even in the hundred nanomolar range, which is to our knowledge the highest affinity ever observed for HSA and its ligands. The displacement of warfarin, a reference drug binding to HSA, by the quinide has also been demonstrated. (C) 2014 Elsevier Ltd. All rights reserved.