benzyl (1S,2S)-5-(2-methoxy-2-oxoethylidene)-2-(4-phenylpiperazine-1-carbonyl)cyclohexane-1-carboxylate | 851001-17-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪烷类
• 英文名称: benzyl (1S,2S)-5-(2-methoxy-2-oxoethylidene)-2-(4-phenylpiperazine-1-carbonyl)cyclohexane-1-carboxylate
• CAS: 851001-17-7
• 化学式: C₂₈H₃₂N₂O₅
• 分子量: 476.572
• InChiKey: MAVOICDNFLCBHV-DQEYMECFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  35
• 可旋转键数：
  8
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  76.2
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  benzyl (1S,2S)-5-(2-methoxy-2-oxoethylidene)-2-(4-phenylpiperazine-1-carbonyl)cyclohexane-1-carboxylate 在 palladium 10% on activated carbon 、 氢气 作用下， 以 甲醇 为溶剂， 生成 (1S,2S)-5-(2-methoxy-2-oxoethyl)-2-(4-phenylpiperazine-1-carbonyl)cyclohexane-1-carboxylic acid
  参考文献：
  名称：

  Compelling P1 substituent affect on metalloprotease binding profile enables the design of a novel cyclohexyl core scaffold with excellent MMP selectivity and HER-2 sheddase inhibition

  摘要：

  A serendipitous discovery that the metalloprotease binding pro. le of a novel class of 2-carboxamide-3-hydroxamic acid piperidines could be significantly attenuated by the modi. cation of the unexplored P1 substituent enabled the design and synthesis of a novel 2-carboxamide-1-hydroxamic acid cyclohexyl scaffold core that exhibited excellent HER-2 potency and unprecedented MMP-selectivity that we believe would not have been possible via conventional P1' perturbations. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.04.143
• 作为产物：
  描述：

  N-苯基哌嗪 、 (1S,2S)-4-(2-methoxy-2-oxoethylidene)-2-phenylmethoxycarbonylcyclohexane-1-carboxylic acid 在 N-甲基吗啉 、 (benzotriazo-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以94%的产率得到benzyl (1S,2S)-5-(2-methoxy-2-oxoethylidene)-2-(4-phenylpiperazine-1-carbonyl)cyclohexane-1-carboxylate
  参考文献：
  名称：

  Compelling P1 substituent affect on metalloprotease binding profile enables the design of a novel cyclohexyl core scaffold with excellent MMP selectivity and HER-2 sheddase inhibition

  摘要：

  A serendipitous discovery that the metalloprotease binding pro. le of a novel class of 2-carboxamide-3-hydroxamic acid piperidines could be significantly attenuated by the modi. cation of the unexplored P1 substituent enabled the design and synthesis of a novel 2-carboxamide-1-hydroxamic acid cyclohexyl scaffold core that exhibited excellent HER-2 potency and unprecedented MMP-selectivity that we believe would not have been possible via conventional P1' perturbations. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.04.143

文献信息

• Compelling P1 substituent affect on metalloprotease binding profile enables the design of a novel cyclohexyl core scaffold with excellent MMP selectivity and HER-2 sheddase inhibition
  作者：David M. Burns、Yun-Long Li、Eric Shi、Chunhong He、Meizhong Xu、Jincong Zhuo、Colin Zhang、Ding-Quan Qian、Yanlong Li、Richard Wynn、Maryanne B. Covington、Kamna Katiyar、Cindy A. Marando、Jordan S. Fridman、Peggy Scherle、Steve Friedman、Brian Metcalf、Wenqing Yao

  DOI：10.1016/j.bmcl.2009.04.143

  日期：2009.7

  A serendipitous discovery that the metalloprotease binding pro. le of a novel class of 2-carboxamide-3-hydroxamic acid piperidines could be significantly attenuated by the modi. cation of the unexplored P1 substituent enabled the design and synthesis of a novel 2-carboxamide-1-hydroxamic acid cyclohexyl scaffold core that exhibited excellent HER-2 potency and unprecedented MMP-selectivity that we believe would not have been possible via conventional P1' perturbations. (C) 2009 Elsevier Ltd. All rights reserved.