tert-butyl (5-bromo-2-methyl-1-(phenylsulfonyl)-1H-indol-3-yl)methyl(tert-butoxycarbonyloxy)carbamate | 919295-69-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: tert-butyl (5-bromo-2-methyl-1-(phenylsulfonyl)-1H-indol-3-yl)methyl(tert-butoxycarbonyloxy)carbamate
• 英文别名: [[1-(Benzenesulfonyl)-5-bromo-2-methylindol-3-yl]methyl-[(2-methylpropan-2-yl)oxycarbonyl]amino] tert-butyl carbonate
• CAS: 919295-69-5
• 化学式: C₂₆H₃₁BrN₂O₇S
• 分子量: 595.511
• InChiKey: CXMPKRCQBPSFMV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.5
• 重原子数：
  37
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  113
• 氢给体数：
  0
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  tert-butyl (5-bromo-2-methyl-1-(phenylsulfonyl)-1H-indol-3-yl)methyl(tert-butoxycarbonyloxy)carbamate 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 2.0h， 生成 N-((5-bromo-2-methyl-1(phenylsulfonyl)-1H-indol-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 sodium tetrahydroborate 、 N-溴代丁二酰亚胺(NBS) 、 sodium hydride 、 三苯基膦 作用下， 以 四氢呋喃 、 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 9.25h， 生成 tert-butyl (5-bromo-2-methyl-1-(phenylsulfonyl)-1H-indol-3-yl)methyl(tert-butoxycarbonyloxy)carbamate
  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

文献信息

• Discovery and Refinement of a New Structural Class of Potent Peptide Deformylase Inhibitors
  作者：Adrien Boularot、Carmela Giglione、Sylvain Petit、Yann Duroc、Rodolphe Alves de Sousa、Valéry Larue、Thierry Cresteil、Frédéric Dardel、Isabelle Artaud、Thierry Meinnel

  DOI：10.1021/jm060910c

  日期：2007.1.1

  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.