4-phosphorylcinnamic acid | 178432-36-5

• 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: 4-phosphorylcinnamic acid
• CAS: 178432-36-5
• 化学式: C₉H₉O₆P
• 分子量: 244.141
• InChiKey: YHJCTVKDEJINEY-ZZXKWVIFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.26
• 重原子数：
  16.0
• 可旋转键数：
  4.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  104.06
• 氢给体数：
  3.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  Fmoc-Ser(CO2-nitrophenyl)-NHBn 、 Fmoc-L-亮氨酸 、 Fmoc-L-脯氨酸 、 4-phosphorylcinnamic acid 生成 (S)-3-(benzylamino)-2-((S)-1-((S)-4-methyl-2-(3-(4-(phosphonooxy)phenyl)acrylamido)pentanoyl)pyrrolidine-2-carboxamido)-3-oxopropyl carbamate
  参考文献：
  名称：

  Solid-phase synthesis of Stat3 inhibitors incorporating O-carbamoylserine and O-carbamoylthreonine as glutamine mimics

  摘要：

  O-Carbamoyiserine and O-carbamoylthreonine are glutamine analogues that were incorporated into a Stat3 inhibitory peptide to probe the requirements of Gin at the pY+3 position. Fmoc-Ser-NHBn and Fmoc-Thr-NHBn were converted to nitrophenyl carbonates and were attached to Rink resin via a side-chain carbamate linkage. After assembly of the peptide, acid treatment resulted in O-carbamoylserine and O-carbamoylthreonine-containing peptides. The order of affinity for Stat3 was Gin > Ser (CONH2) > Thr(CONH2) suggesting a relatively tight binding pocket for the side chain of glutamine. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2006.10.099
• 作为产物：
  描述：

  tert-butyldimethylsilyl (2E)-3-(4-hydroxyphenyl)acrylate 在 bis(trimethylsilyl)trifluoroacetamide 、 碘代三甲硅烷 、 四溴化碳 、 碳酸氢钠 、 三乙胺 、 sodium sulfite 作用下， 以 四氢呋喃 、 乙醚 、 二氯甲烷 为溶剂， 反应 3.0h， 生成 4-phosphorylcinnamic acid
  参考文献：
  名称：

  新型磷酸酪氨酸模拟物的一般合成

  摘要：

  描述了一种由相应的酚类前体制备各种磷酸酪氨酸模拟物的简单通用方法。酚酸的原位甲硅烷基化，然后用Et 3 N / CBr 4 / HP（O）（OEt）2处理可提供磷酸二乙酯中间体（36–96％），在用BSTFA / TMSI处理后可以定量地将其干净地脱保护提供新型的磷酸酪氨酸模拟物。

  DOI：

  10.1016/0040-4039(96)00666-1

文献信息

• INHIBITORS OF STAT3 AND USES THEREOF
  申请人：McMurray John S.

  公开号：US20120035114A1

  公开（公告）日：2012-02-09

  Compounds which inhibit the activity of signal transducer and activator of transcription 3 (STAT3) are provided together with methods of making and using the same. The compounds are designed to bind to the SH2 domain of STAT3, preventing STAT3 from binding to receptors for interleukin-6 family cytokines, growth factors such as the platelet-derived growth factor, the epidermal growth factor, vascular endothelial growth factor, and other signaling molecules such as leptin. Blocking these interactions prevents STAT3 from being phosphorylated on Tyr705, which is required for the dimerization of STAT3, translocation to the nucleus, binding to STAT3 response elements on promotors, and transcription of genes. In addition to these activities, binding to the SH2 domain of STAT3 breaks up pre-formed dimmers, thereby preventing the transcriptional activity of the inhibitor.

  本发明提供了抑制信号转导与激活转录因子3 (STAT3) 活性的化合物，以及制备和使用这些化合物的方法。这些化合物被设计成结合STAT3的SH2结构域，防止STAT3与白细胞介素6家族细胞因子、血小板源性生长因子、表皮生长因子、血管内皮生长因子等生长因子和瘦素等信号分子的受体结合。阻断这些相互作用可防止STAT3在Tyr705位点磷酸化，这是STAT3二聚化、向细胞核转位、结合启动子上的STAT3响应元件和基因转录所必需的。除了这些作用，结合STAT3的SH2结构域还可以分解已形成的二聚体，从而防止抑制剂的转录活性。
• US8841257B2
  申请人：——

  公开号：US8841257B2

  公开（公告）日：2014-09-23
• [EN] INHIBITORS OF STAT3 AND USES THEREOF<br/>[FR] INHIBITEURS DU STAT3 ET LEURS UTILISATIONS
  申请人：UNIV TEXAS

  公开号：WO2010118309A2

  公开（公告）日：2010-10-14

  Compounds which inhibit the activity of signal transducer and activator of transcription 3 (STAT3) are provided together with methods of making and using the same. The compounds are designed to bind to the SH2 domain of STAT3, preventing STAT3 from binding to receptors for interleukin-6 family cytokines, growth factors such as the platelet-derived growth factor, the epidermal growth factor, vascular endothelial growth factor, and other signaling molecules such as leptin. Blocking these interactions prevents STAT3 from being phosphorylated on Tyr705, which is required for the dimerization of STAT3, translocation to the nucleus, binding to STAT3 response elements on promotors, and transcription of genes. In addition to these activities, binding to the SH2 domain of STAT3 breaks up pre-formed dimmers, thereby preventing the transcriptional activity of the inhibitor.