N-(2-Hydroxy-phenyl)-3-trifluoromethyl-benzamide | 33089-87-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: N-(2-Hydroxy-phenyl)-3-trifluoromethyl-benzamide
• 英文别名: N-(2-hydroxyphenyl)-3-(trifluoromethyl)benzamide
• CAS: 33089-87-1
• 化学式: C₁₄H₁₀F₃NO₂
• 分子量: 281.234
• InChiKey: XAOGTUWNLPXZIM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  20
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.07
• 拓扑面积：
  49.3
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-(2-Hydroxy-phenyl)-3-trifluoromethyl-benzamide 在 对甲苯磺酸 作用下， 以 xylene 为溶剂， 反应 5.0h， 以109 mg的产率得到2-(3-(trifluoromethyl)phenyl)benzo[d]oxazole
  参考文献：
  名称：

  Biochemical and Structural Evaluation of Highly Selective 2-Arylbenzoxazole-Based Transthyretin Amyloidogenesis Inhibitors

  摘要：

  To develop potent transthyretin (TTR) amyloidogenesis inhibitors that also display high binding selectivity in blood, it proves useful to systematically optimize each of the three substructural elements that comprise a typical inhibitor: the two aryl rings and the linker joining them. In the first study, described herein, structural modifications to one aryl ring were evaluated by screening a library of 2-arylbenzoxazoles bearing thyroid hormone-like aryl substituents on the 2-aryl ring. Several potent and highly selective amyloidogenesis inhibitors were identified that exhibit minimal thyroid hormone nuclear receptor and COX-1 binding. High resolution crystal structures (1.3-1.5 angstrom) of three inhibitors (2f, 4f, and 4d) in complex with TTR were obtained to characterize their binding orientation. Collectively, the results demonstrate that thyroid hormone-like substitution patterns on one aryl ring lead to potent and highly selective TTR amyloidogenesis inhibitors that lack undesirable thyroid hormone receptor or COX-1 binding.

  DOI：

  10.1021/jm0708735
• 作为产物：
  描述：

  3-(三氟甲基)苯甲酰氯 、 2-氨基苯酚 在 吡啶 作用下， 以 xylene 为溶剂， 反应 1.0h， 生成 N-(2-Hydroxy-phenyl)-3-trifluoromethyl-benzamide
  参考文献：
  名称：

  Biochemical and Structural Evaluation of Highly Selective 2-Arylbenzoxazole-Based Transthyretin Amyloidogenesis Inhibitors

  摘要：

  To develop potent transthyretin (TTR) amyloidogenesis inhibitors that also display high binding selectivity in blood, it proves useful to systematically optimize each of the three substructural elements that comprise a typical inhibitor: the two aryl rings and the linker joining them. In the first study, described herein, structural modifications to one aryl ring were evaluated by screening a library of 2-arylbenzoxazoles bearing thyroid hormone-like aryl substituents on the 2-aryl ring. Several potent and highly selective amyloidogenesis inhibitors were identified that exhibit minimal thyroid hormone nuclear receptor and COX-1 binding. High resolution crystal structures (1.3-1.5 angstrom) of three inhibitors (2f, 4f, and 4d) in complex with TTR were obtained to characterize their binding orientation. Collectively, the results demonstrate that thyroid hormone-like substitution patterns on one aryl ring lead to potent and highly selective TTR amyloidogenesis inhibitors that lack undesirable thyroid hormone receptor or COX-1 binding.

  DOI：

  10.1021/jm0708735

文献信息

• Supported Pd-catalyzed ring opening and chemoselective aminocarbonylative coupling of benzoxazoles with aryl iodides
  作者：Pushkar Mehara、Ajay Kumar Sharma、Ashish Kumar、Poonam Sharma、Pralay Das

  DOI：10.1039/d4cy00070f

  日期：——

  A tandem approach using polystyrene supported Pd catalyzed ring opening aminocarbonylative coupling of benzoxazoles with aryl iodides has been developed for the synthesis of N-(2-hydroxyphenyl)benzamides using solid oxalic acid as the CO source.

  以固体草酸为 CO 源，开发了一种串联方法，利用聚苯乙烯支撑的钯催化苯并恶唑与芳基碘化物的开环氨基羰基偶联合成 N-(2-羟基苯基)苯甲酰胺。
• US3979411A
  申请人：——

  公开号：US3979411A

  公开（公告）日：1976-09-07
• Biochemical and Structural Evaluation of Highly Selective 2-Arylbenzoxazole-Based Transthyretin Amyloidogenesis Inhibitors
  作者：Steven M. Johnson、Stephen Connelly、Ian A. Wilson、Jeffery W. Kelly

  DOI：10.1021/jm0708735

  日期：2008.1.1

  To develop potent transthyretin (TTR) amyloidogenesis inhibitors that also display high binding selectivity in blood, it proves useful to systematically optimize each of the three substructural elements that comprise a typical inhibitor: the two aryl rings and the linker joining them. In the first study, described herein, structural modifications to one aryl ring were evaluated by screening a library of 2-arylbenzoxazoles bearing thyroid hormone-like aryl substituents on the 2-aryl ring. Several potent and highly selective amyloidogenesis inhibitors were identified that exhibit minimal thyroid hormone nuclear receptor and COX-1 binding. High resolution crystal structures (1.3-1.5 angstrom) of three inhibitors (2f, 4f, and 4d) in complex with TTR were obtained to characterize their binding orientation. Collectively, the results demonstrate that thyroid hormone-like substitution patterns on one aryl ring lead to potent and highly selective TTR amyloidogenesis inhibitors that lack undesirable thyroid hormone receptor or COX-1 binding.