1-bromomethyl-3-decyloxy-benzene | 859454-40-3

• 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: 1-bromomethyl-3-decyloxy-benzene
• 英文别名: 1-(Bromomethyl)-3-decoxybenzene
• CAS: 859454-40-3
• 化学式: C₁₇H₂₇BrO
• mdl: MFCD18587297
• 分子量: 327.305
• InChiKey: LAMXOHCSIYLWCO-UHFFFAOYSA-N

物化性质

• 沸点：
  385.5±17.0 °C(predicted)
• 密度：
  1.122±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  7
• 重原子数：
  19
• 可旋转键数：
  11
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.647
• 拓扑面积：
  9.2
• 氢给体数：
  0
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  1-bromomethyl-3-decyloxy-benzene 在 盐酸 、 溶剂黄146 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基乙酰胺 为溶剂， 生成 1-(3-(decyloxy)benzyl)-1,2-dihydro-4-hydroxy-2-oxopyridine-3-carboxylic acid
  参考文献：
  名称：

  HIV-1 Integrase Inhibitor-Inspired Antibacterials Targeting Isoprenoid Biosynthesis

  摘要：

  We report the discovery of antibacterial leads, keto- and diketo-acids, targeting two prenyl transferases: undecaprenyl diphosphate synthase (UPPS) and dehydrosqualene synthase (CrtM). The leads were suggested by the observation that keto- and diketo-acids bind to the active site Mg2+/Asp domain in HIV-1 integrase, and similar domains are present in prenyl transferases. We report the X-ray crystallographic structures of one diketo-acid and one keto-acid bound to CrtM, which supports the Mg2+ binding hypothesis, together with the X-ray structure of one diketo-acid bound to UPPS. In all cases, the inhibitors bind to a farnesyl diphosphate substrate-binding site. Compound 45 had cell growth inhibition MIC90 values of similar to 250-500 ng/mL against Staphylococcus aureus, 500 ng/mL against Bacillus anthracis, 4 mu g/mL against Listeria monocytogenes and Enterococcus faecium, and 1 mu g/mL against Streptococcus pyogenes M1 but very little activity against Escherichia coli (DH5 alpha, K12) or human cell lines.

  DOI：

  10.1021/ml300038t

文献信息

• Inhibition of Geranylgeranyl Diphosphate Synthase by Bisphosphonates: A Crystallographic and Computational Investigation
  作者：Michael P. Hudock、Yonghui Zhang、Rey-Ting Guo、Rong Cao、Joo Hwan No、Po-Huang Liang、Tzu-Ping Ko、Tao-Hsin Chang、Shiou-chi Chang、Yongcheng Song、Jordan Axelson、Anup Kumar、Andrew H.-J. Wang、Eric Oldfield

  DOI：10.1021/jm800325y

  日期：2008.9.25

  We report the X-ray structures of several bisphosphonate inhibitors of geranylgeranyl diphosphate synthase, a target for anticancer drugs. Bisphosphonates containing unbranched side chains bind to either the farnesyl diphosphate (FPP) substrate site, the geranylgeranyl diphosphate (GGPP) product site, and in one case, both sites, with the bisphosphonate moiety interacting with 3 Mg2+ that occupy the same position as found in FPP synthase. However, each of three "V-shaped" bisphosphonates bind to both the FPP and GGPP sites. Using the Glide program, we reproduced the binding modes of 10 bisphosphonates with an rms error of 1.3 angstrom. Activities of the bisphosphonates in GGPPS inhibition were predicted with an overall error of 2x by using a comparative molecular similarity analysis based on a docked-structure alignment. These results show that some GGPPS inhibitors can occupy both substrate and product site and that binding modes as well as activity can be accurately predicted, facilitating the further development of GGPPS inhibitors as anticancer agents.
• HIV-1 Integrase Inhibitor-Inspired Antibacterials Targeting Isoprenoid Biosynthesis
  作者：Yonghui Zhang、Fu-Yang Lin、Kai Li、Wei Zhu、Yi-Liang Liu、Rong Cao、Ran Pang、Eunhae Lee、Jordan Axelson、Mary Hensler、Ke Wang、Katie J. Molohon、Yang Wang、Douglas A. Mitchell、Victor Nizet、Eric Oldfield

  DOI：10.1021/ml300038t

  日期：2012.5.10

  We report the discovery of antibacterial leads, keto- and diketo-acids, targeting two prenyl transferases: undecaprenyl diphosphate synthase (UPPS) and dehydrosqualene synthase (CrtM). The leads were suggested by the observation that keto- and diketo-acids bind to the active site Mg2+/Asp domain in HIV-1 integrase, and similar domains are present in prenyl transferases. We report the X-ray crystallographic structures of one diketo-acid and one keto-acid bound to CrtM, which supports the Mg2+ binding hypothesis, together with the X-ray structure of one diketo-acid bound to UPPS. In all cases, the inhibitors bind to a farnesyl diphosphate substrate-binding site. Compound 45 had cell growth inhibition MIC90 values of similar to 250-500 ng/mL against Staphylococcus aureus, 500 ng/mL against Bacillus anthracis, 4 mu g/mL against Listeria monocytogenes and Enterococcus faecium, and 1 mu g/mL against Streptococcus pyogenes M1 but very little activity against Escherichia coli (DH5 alpha, K12) or human cell lines.