5-丁基-1,3,4-噁二唑-2-胺 | 52838-38-7

• 分子结构分类: 有机化合物 - 有机氮化合物
• 中文名称: 5-丁基-1,3,4-噁二唑-2-胺
• 中文别名: 5-丁基-1,3,4-恶二唑-2-胺
• 英文名称: 2-Amino-5-n-butyl-1,3,4-oxadiazol
• 英文别名: 5-butyl-1,3,4-oxadiazol-2-amine
• CAS: 52838-38-7
• 化学式: C₆H₁₁N₃O
• mdl: MFCD09261277
• 分子量: 141.173
• InChiKey: JANUDBLANRHSLI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  10
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.666
• 拓扑面积：
  64.9
• 氢给体数：
  1
• 氢受体数：
  4

安全信息

• 海关编码：
  2934999090

反应信息

• 作为反应物：
  描述：

  6-硝基藜芦酸 、 5-丁基-1,3,4-噁二唑-2-胺 在 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以25%的产率得到N-(5-butyl-1,3,4-oxadiazol-2-yl)-4,5-dimethoxy-2-nitrobenzamide
  参考文献：
  名称：

  Lipoprotein Signal Peptidase Inhibitors with Antibiotic Properties Identified through Design of a Robust In Vitro HT Platform

  摘要：

  As resistance to antibiotics increases, the exploration of new targets and strategies to combat pathogenic bacteria becomes more urgent. Ideal protein targets are required for viability across many species, are unique to prokaryotes to limit effects on the host, and have robust assays to quantitate activity and identify inhibitors. Lipoprotein signal peptidase (Lsp) is a transmembrane aspartyl protease required for lipoprotein maturation and comprehensively fits these criteria. Here, we have developed the first in vitro high-throughput assay to monitor proteolysis by Lsp. We employed our high-throughput screen assay against 646,275 compounds to discover inhibitors of Lsp and synthesized a range of analogs to generate molecules with nanomolar half maximal inhibitory concentration values. Importantly, our inhibitors are effective in preventing the growth of E. coli cultures in the presence of outermembrane permeabilizer PMBN and should facilitate development of antibacterial agents with a novel mechanism of action to treat antibiotic-resistant bacteria.

  DOI：

  10.1016/j.chembiol.2017.12.011

文献信息

• Gehlen,H.; Just,M., Justus Liebigs Annalen der Chemie, 1966, vol. 692, p. 151 - 165
  作者：Gehlen,H.、Just,M.

  DOI：——

  日期：——
• Gehlen,H.; Just,M., Justus Liebigs Annalen der Chemie, 1967, vol. 703, p. 131 - 135
  作者：Gehlen,H.、Just,M.

  DOI：——

  日期：——
• HUSAIN, M. I.;GUPTA, K. B., INDIAN J. PARM. SCI., 1981, 43, N 2, 44-46
  作者：HUSAIN, M. I.、GUPTA, K. B.

  DOI：——

  日期：——
• Lipoprotein Signal Peptidase Inhibitors with Antibiotic Properties Identified through Design of a Robust In Vitro HT Platform
  作者：Seiya Kitamura、Anna Owensby、Daniel Wall、Dennis W. Wolan

  DOI：10.1016/j.chembiol.2017.12.011

  日期：2018.3

  As resistance to antibiotics increases, the exploration of new targets and strategies to combat pathogenic bacteria becomes more urgent. Ideal protein targets are required for viability across many species, are unique to prokaryotes to limit effects on the host, and have robust assays to quantitate activity and identify inhibitors. Lipoprotein signal peptidase (Lsp) is a transmembrane aspartyl protease required for lipoprotein maturation and comprehensively fits these criteria. Here, we have developed the first in vitro high-throughput assay to monitor proteolysis by Lsp. We employed our high-throughput screen assay against 646,275 compounds to discover inhibitors of Lsp and synthesized a range of analogs to generate molecules with nanomolar half maximal inhibitory concentration values. Importantly, our inhibitors are effective in preventing the growth of E. coli cultures in the presence of outermembrane permeabilizer PMBN and should facilitate development of antibacterial agents with a novel mechanism of action to treat antibiotic-resistant bacteria.