| 1478871-84-9

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• CAS: 1478871-84-9
• 化学式: C₇₂H₁₁₂F₃N₁₃O₂₃
• 分子量: 1584.75
• InChiKey: PFYOEIKWJDLPFT-RQZISVTLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.31
• 重原子数：
  111.0
• 可旋转键数：
  57.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.72
• 拓扑面积：
  458.04
• 氢给体数：
  8.0
• 氢受体数：
  28.0

反应信息

• 作为反应物：
  描述：

  在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 1.5h， 生成
  参考文献：
  名称：

  Synthesis and Evaluation of a Photoactive Probe with a Multivalent Carbohydrate for Capturing Carbohydrate–Lectin Interactions

  摘要：

  Lectins are ubiquitous carbohydrate-binding proteins of nonimmune origin that are characterized by their specific recognition of defined monosaccharide or oligosaccharide structures. However, the use of carbohydrates to study lectin has been restricted by the weak binding affinity and noncovalent character of the interaction between carbohydrates and lectin. In this report, we designed and synthesized a multifunctional photoaffinity reagent composed of a trialkyne chain, a masked latent amine group, and a photoreactive 3-trifluoromethyl-3phenyl-diazirine group in high overall yield. Two well-defined chemistries, Huisgen-Sharpless click chemistry and amide bond coupling, were the key steps for installing the multivalent character and tag in our designed photoaffinity probe. The photolabeling results demonstrated that the designed probe selectively labeled the target lectin, RCA(120) (Ricinus communis Agglutinin), in an E. coli lysate and an asialoglycoprotein receptor (ASGP-R) on intact HepG2 cell membranes. Moreover, the probe also enabled the detection of weak protein protein interactions between RCA(120) and ovalbumin (OVA).

  DOI：

  10.1021/bc400306g
• 作为产物：
  描述：

  tert-butyl (S)-(2,8,15,22,25,32-hexaoxo-23-(3-oxo-3-((2-(prop-2-yn-1-yloxy)ethyl)amino)propyl)-1-(4-(3-(trifluoromethyl)-3H-diazirin-3-yl)phenoxy)-3,7,14,21,24,31-hexaazaheptatriacontan-37-yl)carbamate 、 1-azido-3,6-dioxaoct-8-yl 2,3,4,6-tetra-O-acetyl-β-D-galactopyranoside 在 N,N-二异丙基乙胺 、 copper(l) iodide 、 copper(II) sulfate 、 sodium ascorbate 作用下， 以 乙醇 、 水 、 叔丁醇 为溶剂， 反应 6.08h， 以72%的产率得到
  参考文献：
  名称：

  Synthesis and Evaluation of a Photoactive Probe with a Multivalent Carbohydrate for Capturing Carbohydrate–Lectin Interactions

  摘要：

  Lectins are ubiquitous carbohydrate-binding proteins of nonimmune origin that are characterized by their specific recognition of defined monosaccharide or oligosaccharide structures. However, the use of carbohydrates to study lectin has been restricted by the weak binding affinity and noncovalent character of the interaction between carbohydrates and lectin. In this report, we designed and synthesized a multifunctional photoaffinity reagent composed of a trialkyne chain, a masked latent amine group, and a photoreactive 3-trifluoromethyl-3phenyl-diazirine group in high overall yield. Two well-defined chemistries, Huisgen-Sharpless click chemistry and amide bond coupling, were the key steps for installing the multivalent character and tag in our designed photoaffinity probe. The photolabeling results demonstrated that the designed probe selectively labeled the target lectin, RCA(120) (Ricinus communis Agglutinin), in an E. coli lysate and an asialoglycoprotein receptor (ASGP-R) on intact HepG2 cell membranes. Moreover, the probe also enabled the detection of weak protein protein interactions between RCA(120) and ovalbumin (OVA).

  DOI：

  10.1021/bc400306g