N-(4-(oxazol-5-yl)benzyl)acetamide | 1422984-95-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: N-(4-(oxazol-5-yl)benzyl)acetamide
• 英文别名: N-[[4-(1,3-oxazol-5-yl)phenyl]methyl]acetamide
• CAS: 1422984-95-9
• 化学式: C₁₂H₁₂N₂O₂
• 分子量: 216.239
• InChiKey: QIVURCIUAPRKEQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  55.1
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  4-(噁唑-5-基)苄基氨基甲酸叔丁酯 在 三乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 生成 N-(4-(oxazol-5-yl)benzyl)acetamide
  参考文献：
  名称：

  Is NMR Fragment Screening Fine-Tuned to Assess Druggability of Protein–Protein Interactions?

  摘要：

  Modulation of protein-protein interactions (PPIs) with small molecules has been hampered by a lack of lucid methods capable of reliably identifying high-quality hits. In fragment screening, the low ligand efficiencies associated with PPI target sites pose significant challenges to fragment binding detection. Here, we investigate the requirements for ligand-based NMR techniques to detect rule-of-three compliant fragments that form part of known high affinity inhibitors of the PPI between the von Hippel-Lindau protein and the alpha subunit of hypoxia-inducible factor 1 (pVHL:HIF-1 alpha). Careful triaging allowed rescuing weak but specific binding of fragments that would otherwise escape detection at this PPI. Further structural information provided by saturation transfer difference (STD) group epitope mapping, protein-based NMR, competitive isothermal titration calorimetry (ITC), and X-ray crystallography confirmed the binding mode of the rescued fragments. Our findings have important implications for PPI druggability assessment by fragment screening as they reveal an accessible threshold for fragment detection and validation.

  DOI：

  10.1021/ml400296c