[3R(1'R,4R)]-3-(1'-hydroxy-ethyl)-4-octylsulfanyl-azetidin-2-one | 1067890-56-5

• 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: [3R(1'R,4R)]-3-(1'-hydroxy-ethyl)-4-octylsulfanyl-azetidin-2-one
• CAS: 1067890-56-5
• 化学式: C₁₃H₂₅NO₂S
• 分子量: 259.413
• InChiKey: RIAYXBBFZDNLHY-NQBHXWOUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.53
• 重原子数：
  17.0
• 可旋转键数：
  9.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  49.33
• 氢给体数：
  2.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  [3R(1'R,4R)]-3-(1'-hydroxy-ethyl)-4-octylsulfanyl-azetidin-2-one 、 己基-5-壬基氯 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 1.17h， 以19%的产率得到[3R(1'R,4R)]-hex-5-ynoic acid 1'-(2-octylsulfanyl-4-oxo-azetidin-3-yl)-ethyl ester
  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
• 作为产物：
  描述：

  [3R(1'R,4R)]-3-[1'-(tert-butyl-dimethyl-silanyloxy)-ethyl]-4-octylsulfanyl-azetidin-2-one 在 四丁基氟化铵 作用下， 以 四氢呋喃 为溶剂， 以47%的产率得到[3R(1'R,4R)]-3-(1'-hydroxy-ethyl)-4-octylsulfanyl-azetidin-2-one
  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