Acetic acid (2R,3R)-1-benzylcarbamoyl-3-methyl-4-oxo-azetidin-2-yl ester

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酰胺类
• 英文名称: Acetic acid (2R,3R)-1-benzylcarbamoyl-3-methyl-4-oxo-azetidin-2-yl ester
• 英文别名: [(2R,3R)-1-(benzylcarbamoyl)-3-methyl-4-oxoazetidin-2-yl] acetate
• 化学式: C₁₄H₁₆N₂O₄
• 分子量: 276.292
• InChiKey: VDLCVJDQYNSMSN-TVQRCGJNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  20
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  75.7
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  4-acetoxy-3-methyl-azetidin-2-one 、 异氰酸苄酯 在 4-二甲氨基吡啶 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 生成 Acetic acid (2R,3S)-1-benzylcarbamoyl-3-methyl-4-oxo-azetidin-2-yl ester 、 Acetic acid (2R,3R)-1-benzylcarbamoyl-3-methyl-4-oxo-azetidin-2-yl ester
  参考文献：
  名称：

  Design and synthesis of monocyclic β-lactams as mechanism-based inhibitors of human cytomegalovirus protease

  摘要：

  Mechanism based inhibitors of HCMV protease have been designed based on the monocyclic beta-lactam nucleus, which have been shown to acylate the viral enzyme in a time dependant manner. SAR in a series of monocyclic beta-lactam N-ureas, has defined the size and relative stereochemisty of the C-3 substituent producing a low micromolar inhibitor 17b with good aqueous stability and selectivity over the mammalian serine proteases. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(98)00032-8

文献信息

• Design and synthesis of monocyclic β-lactams as mechanism-based inhibitors of human cytomegalovirus protease
  作者：Alan D. Borthwick、Gordon Weingarten、Terry M. Haley、Mirek Tomaszewski、Wei Wang、Zhouhan Hu、Jean Bedard、Haloun Jin、Leonard Yuen、Tarek S. Mansour

  DOI：10.1016/s0960-894x(98)00032-8

  日期：1998.2

  Mechanism based inhibitors of HCMV protease have been designed based on the monocyclic beta-lactam nucleus, which have been shown to acylate the viral enzyme in a time dependant manner. SAR in a series of monocyclic beta-lactam N-ureas, has defined the size and relative stereochemisty of the C-3 substituent producing a low micromolar inhibitor 17b with good aqueous stability and selectivity over the mammalian serine proteases. (C) 1998 Elsevier Science Ltd. All rights reserved.