3-(3-Cyclohexylisoxazol-4-yl)-5-phenyl-thiophene-2-carboxylic acid | 1243356-87-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 噻吩类
• 英文名称: 3-(3-Cyclohexylisoxazol-4-yl)-5-phenyl-thiophene-2-carboxylic acid
• 英文别名: 3-(3-cyclohexyl-1,2-oxazol-4-yl)-5-phenylthiophene-2-carboxylic acid
• CAS: 1243356-87-7
• 化学式: C₂₀H₁₉NO₃S
• 分子量: 353.442
• InChiKey: ARQOQPBWYJBFHM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.4
• 重原子数：
  25
• 可旋转键数：
  4
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  91.6
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  生成 3-(3-Cyclohexylisoxazol-4-yl)-5-phenyl-thiophene-2-carboxylic acid
  参考文献：
  名称：

  Cyclic amide bioisosterism: Strategic application to the design and synthesis of HCV NS5B polymerase inhibitors

  摘要：

  Conformational modeling has been successfully applied to the design of cyclic bioisosteres used to replace a conformationally rigid amide bond in a series of thiophene carboxylate inhibitors of HCV NS5B polymerase. Select compounds were equipotent with the original amide series. Single-point mutant binding studies, in combination with inhibition structure-activity relationships, suggest this new series interacts at the Thumb-II domain of NS5B. Inhibitor binding at the Thumb-II site was ultimately confirmed by solving a crystal structure of 8b complexed with NS5B. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.06.008

文献信息

• Cyclic amide bioisosterism: Strategic application to the design and synthesis of HCV NS5B polymerase inhibitors
  作者：Hanbiao Yang、Robert T. Hendricks、Nidhi Arora、Dov Nitzan、Calvin Yee、Matthew C. Lucas、Yanli Yang、Amy Fung、Sonal Rajyaguru、Seth F. Harris、Vincent J.P. Leveque、Julie Q. Hang、Sophie Le Pogam、Deborah Reuter、Gisele A. Tavares

  DOI：10.1016/j.bmcl.2010.06.008

  日期：2010.8

  Conformational modeling has been successfully applied to the design of cyclic bioisosteres used to replace a conformationally rigid amide bond in a series of thiophene carboxylate inhibitors of HCV NS5B polymerase. Select compounds were equipotent with the original amide series. Single-point mutant binding studies, in combination with inhibition structure-activity relationships, suggest this new series interacts at the Thumb-II domain of NS5B. Inhibitor binding at the Thumb-II site was ultimately confirmed by solving a crystal structure of 8b complexed with NS5B. (C) 2010 Elsevier Ltd. All rights reserved.