6-Bromonaphthalene-2-carbonyl azide | 330803-80-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 6-Bromonaphthalene-2-carbonyl azide
• CAS: 330803-80-0
• 化学式: C₁₁H₆BrN₃O
• 分子量: 276.092
• InChiKey: KVTHQRHKUNPZTC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.7
• 重原子数：
  16
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  31.4
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  6-Bromonaphthalene-2-carbonyl azide 以 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 4.0h， 生成 6-溴-2-氨基萘
  参考文献：
  名称：

  Design, synthesis and biological activity of novel non-amidine factor Xa inhibitors. Part 1: P1 structure–activity relationships of the substituted 1-(2-Naphthyl)-1H-pyrazole-5-carboxylamides

  摘要：

  Based on DuPont Pharmaceuticals' monobenzamidine lead structure SN429, we have designed the biphenyl 1-(2-naphthyl)-1H-pyrazole-5-carboxylamides as a novel series of non-basic factor Xa inhibitors. We have discovered that the displacement of the benzamidine moiety with substituted 2-naphthyl structures not only results in highly potent factor Xa inhibitors, but also significantly increases their enzyme specificity and oral bioavailability. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(02)00239-1
• 作为产物：
  描述：

  6-bromonaphthalene-2-carbonyl chloride 在 sodium azide 作用下， 以 1,4-二氧六环 为溶剂， 反应 2.0h， 生成 6-Bromonaphthalene-2-carbonyl azide
  参考文献：
  名称：

  Design, synthesis and biological activity of novel non-amidine factor Xa inhibitors. Part 1: P1 structure–activity relationships of the substituted 1-(2-Naphthyl)-1H-pyrazole-5-carboxylamides

  摘要：

  Based on DuPont Pharmaceuticals' monobenzamidine lead structure SN429, we have designed the biphenyl 1-(2-naphthyl)-1H-pyrazole-5-carboxylamides as a novel series of non-basic factor Xa inhibitors. We have discovered that the displacement of the benzamidine moiety with substituted 2-naphthyl structures not only results in highly potent factor Xa inhibitors, but also significantly increases their enzyme specificity and oral bioavailability. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(02)00239-1

文献信息

• Design, synthesis and biological activity of novel non-amidine factor Xa inhibitors. Part 1: P1 structure–activity relationships of the substituted 1-(2-Naphthyl)-1H-pyrazole-5-carboxylamides
  作者：Zhaozhong J. Jia、Yanhong Wu、Wenrong Huang、Erick Goldman、Penglie Zhang、John Woolfrey、Paul Wong、Brian Huang、Uma Sinha、Gary Park、Andrea Reed、Robert M. Scarborough、Bing-Yan Zhu

  DOI：10.1016/s0960-894x(02)00239-1

  日期：2002.6

  Based on DuPont Pharmaceuticals' monobenzamidine lead structure SN429, we have designed the biphenyl 1-(2-naphthyl)-1H-pyrazole-5-carboxylamides as a novel series of non-basic factor Xa inhibitors. We have discovered that the displacement of the benzamidine moiety with substituted 2-naphthyl structures not only results in highly potent factor Xa inhibitors, but also significantly increases their enzyme specificity and oral bioavailability. (C) 2002 Elsevier Science Ltd. All rights reserved.
• Structure–Activity Studies on Splitomicin Derivatives as Sirtuin Inhibitors and Computational Prediction of Binding Mode
  作者：Robert C. Neugebauer、Urszula Uchiechowska、Rene Meier、Henning Hruby、Vassil Valkov、Eric Verdin、Wolfgang Sippl、Manfred Jung

  DOI：10.1021/jm700972e

  日期：2008.3.13

  NAD(+)-dependent histone deacetylases (sirtuins) are enzymes that cleave acetyl groups from lysines in histones and other proteins. Potent selective sirtuin inhibitors are interesting tools for the investigation of the biological functions of those enzymes and may be future drugs for the treatment of cancer. Splitomicin was among the first two inhibitors that were discovered for yeast sirtuins but showed rather weak inhibition on human enzymes. We present detailed structure-activity relationships on splitomicin derivatives and their inhibition of recombinant Sirt2. To rationalize our experimental results, ligand docking followed by molecular mechanics Poisson - Boltzmann/surface area (MM-PBSA) calculations were carried out. These analyses suggested a molecular basis for the interaction of the beta-phenylsplitomicins with human Sirt2. Protein-based virtual screening resulted in the identification of a novel Sirt2 inhibitor chemotype. Selected inhibitors showed antiproliferative properties and tubulin hyperacetylation in MCF7 breast cancer cells and are promising candidates for further optimization as potential anticancer drugs.