1-benzyl-N-hydroxy-4-[[4-(2-phenylethynyl)benzoyl]amino]piperidine-4-carboxamide | 1428857-93-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 哌啶类
• 英文名称: 1-benzyl-N-hydroxy-4-[[4-(2-phenylethynyl)benzoyl]amino]piperidine-4-carboxamide
• CAS: 1428857-93-5
• 化学式: C₂₈H₂₇N₃O₃
• 分子量: 453.541
• InChiKey: DFDIUZIKVQMPKA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.5
• 重原子数：
  34
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  81.7
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  4-(苯乙炔基)苯甲酸 在 羟胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 作用下， 以 甲醇 、 水 为溶剂， 反应 12.0h， 生成 1-benzyl-N-hydroxy-4-[[4-(2-phenylethynyl)benzoyl]amino]piperidine-4-carboxamide
  参考文献：
  名称：

  Exploring the UDP pocket of LpxC through amino acid analogs

  摘要：

  Lipopolysaccharide (LPS) biosynthesis is an attractive antibacterial target as it is both conserved and essential for the survival of key pathogenic bacteria. Lipid A is the hydrophobic anchor for LPS and a key structural component of the outer membrane of Gram-negative bacteria. Lipid A biosynthesis is performed in part by a unique zinc dependent metalloamidase, LpxC (UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase), which catalyzes the first non-reversible step in lipid A biosynthesis. The UDP portion of the LpxC substrate-binding pocket has been relatively unexplored. We have designed and evaluated a series of hydroxamate based inhibitors which explore the SAR of substitutions directed into the UDP pocket with a range of substituted α-amino acid based linkers. We also provide the first wild type structure of Pseudomonas aeruginosa LpxC which was utilized in the design of many of these analogs.

  DOI：

  10.1016/j.bmcl.2013.02.055

文献信息

• Exploring the UDP pocket of LpxC through amino acid analogs
  作者：Michael R. Hale、Pamela Hill、Sushmita Lahiri、Matthew D. Miller、Philip Ross、Richard Alm、Ning Gao、Amy Kutschke、Michele Johnstone、Bryan Prince、Jason Thresher、Wei Yang

  DOI：10.1016/j.bmcl.2013.02.055

  日期：2013.4

  Lipopolysaccharide (LPS) biosynthesis is an attractive antibacterial target as it is both conserved and essential for the survival of key pathogenic bacteria. Lipid A is the hydrophobic anchor for LPS and a key structural component of the outer membrane of Gram-negative bacteria. Lipid A biosynthesis is performed in part by a unique zinc dependent metalloamidase, LpxC (UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase), which catalyzes the first non-reversible step in lipid A biosynthesis. The UDP portion of the LpxC substrate-binding pocket has been relatively unexplored. We have designed and evaluated a series of hydroxamate based inhibitors which explore the SAR of substitutions directed into the UDP pocket with a range of substituted α-amino acid based linkers. We also provide the first wild type structure of Pseudomonas aeruginosa LpxC which was utilized in the design of many of these analogs.