7-O-Biotinyl-quercetin | 1334110-96-1

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 黄酮类化合物
• 英文名称: 7-O-Biotinyl-quercetin
• 英文别名: 5-[(3aS,4S,6aR)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-N-[2-[2-[2-[[2-[2-(3,4-dihydroxyphenyl)-3,5-dihydroxy-4-oxochromen-7-yl]oxyacetyl]amino]ethoxy]ethoxy]ethyl]pentanamide
• CAS: 1334110-96-1
• 化学式: C₃₃H₄₀N₄O₁₂S
• 分子量: 716.766
• InChiKey: RDBGOPDIMUUTST-POWSXZFQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  50
• 可旋转键数：
  18
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  260
• 氢给体数：
  8
• 氢受体数：
  13

反应信息

• 作为产物：
  描述：

  [5,7-二乙酰氧基-2-(3,4-二乙酰氧基苯基)-4-氧代苯并吡喃-3-基]乙酸酯 在 咪唑 、 N-甲基-2-二甲氨基乙酰氧肟酸 、 水 、 caesium carbonate 、 苯硫酚 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 13.0h， 生成 7-O-Biotinyl-quercetin
  参考文献：
  名称：

  Biotinylated quercetin as an intrinsic photoaffinity proteomics probe for the identification of quercetin target proteins

  摘要：

  Quercetin is a flavonoid natural product, that is, found in many foods and has been found to have a wide range of medicinal effects. Though a number of quercetin binding proteins have been identified, there has been no systematic approach to identifying all potential targets of quercetin. We describe an O7-biotinylated derivative of quercetin (BioQ) that can act as a photoaffinity proteomics reagent for capturing quercetin binding proteins, which can then be identified by LC-MS/MS. BioQ was shown to inhibit heat induction of HSP70 with almost the same efficiency as quercetin, and to both inhibit and photocrosslink to CK2 kinase, a known target of quercetin involved in activation of the heat shock transcription factor. BioQ was also able to pull down a number of proteins from unheated and heated Jurkat cells following UV irradiation that could be detected by both silver staining and Western blot analysis with an anti-biotin antibody. Analysis of the protein bands by trypsinization and LC-MS/MS led to the identification of heat shock proteins HSP70 and HSP90 as possible quercetin target proteins, along with ubiquitin-activating enzyme, a spliceosomal protein, RuvB-like 2 ATPases, and eukaryotic translation initiation factor 3. In addition, a mitochondrial ATPase was identified that has been previously shown to be a target of quercetin. Most of the proteins identified have also been previously suggested to be potential anticancer targets, suggesting that quercetin's antitumor activity may be due to its ability to inhibit multiple target proteins. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.07.005

文献信息

• Biotinylated quercetin as an intrinsic photoaffinity proteomics probe for the identification of quercetin target proteins
  作者：Rongsheng E. Wang、Clayton R. Hunt、Jiawei Chen、John-Stephen Taylor

  DOI：10.1016/j.bmc.2011.07.005

  日期：2011.8

  Quercetin is a flavonoid natural product, that is, found in many foods and has been found to have a wide range of medicinal effects. Though a number of quercetin binding proteins have been identified, there has been no systematic approach to identifying all potential targets of quercetin. We describe an O7-biotinylated derivative of quercetin (BioQ) that can act as a photoaffinity proteomics reagent for capturing quercetin binding proteins, which can then be identified by LC-MS/MS. BioQ was shown to inhibit heat induction of HSP70 with almost the same efficiency as quercetin, and to both inhibit and photocrosslink to CK2 kinase, a known target of quercetin involved in activation of the heat shock transcription factor. BioQ was also able to pull down a number of proteins from unheated and heated Jurkat cells following UV irradiation that could be detected by both silver staining and Western blot analysis with an anti-biotin antibody. Analysis of the protein bands by trypsinization and LC-MS/MS led to the identification of heat shock proteins HSP70 and HSP90 as possible quercetin target proteins, along with ubiquitin-activating enzyme, a spliceosomal protein, RuvB-like 2 ATPases, and eukaryotic translation initiation factor 3. In addition, a mitochondrial ATPase was identified that has been previously shown to be a target of quercetin. Most of the proteins identified have also been previously suggested to be potential anticancer targets, suggesting that quercetin's antitumor activity may be due to its ability to inhibit multiple target proteins. (C) 2011 Elsevier Ltd. All rights reserved.