5-bromo-2-methyl-1H-indole-3-carbaldehyde oxime | 919295-65-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: 5-bromo-2-methyl-1H-indole-3-carbaldehyde oxime
• 英文别名: N-[(5-bromo-2-methyl-1H-indol-3-yl)methylidene]hydroxylamine
• CAS: 919295-65-1
• 化学式: C₁₀H₉BrN₂O
• 分子量: 253.098
• InChiKey: CNSWXXPPMDTUAI-UHFFFAOYSA-N

物化性质

• 沸点：
  418.2±45.0 °C(Predicted)
• 密度：
  1.63±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  14
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  48.4
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  5-bromo-2-methyl-1H-indole-3-carbaldehyde oxime 在 盐酸 、 sodium cyanoborohydride 作用下， 以 甲醇 、 乙醇 、 四氢呋喃 为溶剂， 生成 N-[2-(5-bromo-2-methyl-1H-indole-3-yl)methyl]hydroxylamine
  参考文献：
  名称：

  Discovery and Refinement of a New Structural Class of Potent Peptide Deformylase Inhibitors

  摘要：

  New classes of antibiotics are urgently needed to counter increasing levels of pathogen resistance. Peptide deformylase (PDF) was originally selected as a specific bacterial target, but a human homologue, the inhibition of which causes cell death, was recently discovered. We developed a dual-screening strategy for selecting highly effective compounds with low inhibition effect against human PDF. We selected a new scaffold in vitro that discriminated between human and bacterial PDFs. Analyses of structure-activity relationships identified potent antibiotics such as 2-(5-bromo-1H-indol-3-yl)-N-hydroxyacetamide (6b) with the same mode of action in vivo as previously identified PDF inhibitors but without the apoptotic effects of these inhibitors in human cells.

  DOI：

  10.1021/jm060910c
• 作为产物：
  描述：

  5-溴-2-甲基吲哚-3-羧醛 在 吡啶 、 盐酸羟胺 作用下， 反应 5.0h， 以100%的产率得到5-bromo-2-methyl-1H-indole-3-carbaldehyde oxime
  参考文献：
  名称：

  Discovery and Refinement of a New Structural Class of Potent Peptide Deformylase Inhibitors

  摘要：

  New classes of antibiotics are urgently needed to counter increasing levels of pathogen resistance. Peptide deformylase (PDF) was originally selected as a specific bacterial target, but a human homologue, the inhibition of which causes cell death, was recently discovered. We developed a dual-screening strategy for selecting highly effective compounds with low inhibition effect against human PDF. We selected a new scaffold in vitro that discriminated between human and bacterial PDFs. Analyses of structure-activity relationships identified potent antibiotics such as 2-(5-bromo-1H-indol-3-yl)-N-hydroxyacetamide (6b) with the same mode of action in vivo as previously identified PDF inhibitors but without the apoptotic effects of these inhibitors in human cells.

  DOI：

  10.1021/jm060910c