hex-5-yn-1-yl (2S,5R,6R)-6-((R)-2-amino-2-phenylacetamido)-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylate | 1067890-46-3

• 英文名称: hex-5-yn-1-yl (2S,5R,6R)-6-((R)-2-amino-2-phenylacetamido)-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylate
• CAS: 1067890-46-3
• 化学式: C₂₂H₂₇N₃O₄S
• 分子量: 429.54
• InChiKey: PKGXFQFKVICMGS-PDOICOKGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.58
• 重原子数：
  30.0
• 可旋转键数：
  8.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  101.73
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为产物：
  描述：

  甲磺酸己-5-炔基酯 、 氨苄西林 以 N,N-二甲基甲酰胺 为溶剂， 以5%的产率得到hex-5-yn-1-yl (2S,5R,6R)-6-((R)-2-amino-2-phenylacetamido)-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylate
  参考文献：
  名称：

  β-Lactams as Selective Chemical Probes for the in Vivo Labeling of Bacterial Enzymes Involved in Cell Wall Biosynthesis, Antibiotic Resistance, and Virulence

  摘要：

  With the development of anti biotic-resistant bacterial strains, infectious diseases have become again a life-threatening problem. One of the reasons for this dilemma is the limited number and breadth of current therapeutic targets for which several resistance strategies have evolved over time. To expand the number of addressable enzyme targets and to understand their function, activity, and regulation, we utilized a chemical proteomic strategy, called activity-based protein profiling (ABPP) pioneered by Cravatt, for the identification of beta-lactam-binding enzymes under in vivo conditions. In this two-tiered strategy, we first prepared a selection of conventional antibiotics for labeling diverse penicillin binding proteins (PBPs) and second introduced a new synthetic generation of beta-lactam probes, which labeled and inhibited a selection of additional PBP unrelated bacterial targets. Among these, the virulence-associated enzyme CIpP and a resistance-associated beta-lactamase were labeled and inhibited by selected probes, indicating that the specificity of beta-lactams can be adjusted to versatile enzyme families with important cellular functions.

  DOI：

  10.1021/ja803349j