methyl 4-[2-[3-[3-(1H-tetrazol-5-yl)phenyl]phenoxy]ethyl]naphthalene-1-carboxylate | 1192505-70-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: methyl 4-[2-[3-[3-(1H-tetrazol-5-yl)phenyl]phenoxy]ethyl]naphthalene-1-carboxylate
• 英文别名: methyl 4-[2-[3-[3-(2H-tetrazol-5-yl)phenyl]phenoxy]ethyl]naphthalene-1-carboxylate
• CAS: 1192505-70-6
• 化学式: C₂₇H₂₂N₄O₃
• 分子量: 450.497
• InChiKey: PAJNTLSRMIQOMW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.8
• 重原子数：
  34
• 可旋转键数：
  8
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  90
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  methyl 4-(2-((3'-cyano-[1,1'-biphenyl]-3-yl)oxy)ethyl)-1-naphthoate 、 三正丁基叠氮化锡 生成 methyl 4-[2-[3-[3-(1H-tetrazol-5-yl)phenyl]phenoxy]ethyl]naphthalene-1-carboxylate
  参考文献：
  名称：

  Structure-based design of substituted biphenyl ethylene ethers as ligands binding in the hydrophobic pocket of gp41 and blocking the helical bundle formation

  摘要：

  A series of substituted biphenyl ethylene ether compounds has been designed to target the gp41 N-trimer in order to inhibit formation of the six-helical bundle that represents the end state of gp41-mediated viral fusion. A size exclusion HPLC based helical bundle formation (HBF) assay was developed to evaluate in vitro inhibitory affinity of the inhibitors. The most potent compound 1 had an IC(50) of 31 mu M. The binding of compound 1 to the proposed hydrophobic pocket of gp41 was further validated by site-directed peptide mutagenesis experiments. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.08.018

文献信息

• Structure-based design of substituted biphenyl ethylene ethers as ligands binding in the hydrophobic pocket of gp41 and blocking the helical bundle formation
  作者：Bin Liu、Rhoda W. Joseph、Bruce D. Dorsey、Robert A. Schiksnis、Katrina Northrop、Marina Bukhtiyarova、Eric B. Springman

  DOI：10.1016/j.bmcl.2009.08.018

  日期：2009.10

  A series of substituted biphenyl ethylene ether compounds has been designed to target the gp41 N-trimer in order to inhibit formation of the six-helical bundle that represents the end state of gp41-mediated viral fusion. A size exclusion HPLC based helical bundle formation (HBF) assay was developed to evaluate in vitro inhibitory affinity of the inhibitors. The most potent compound 1 had an IC(50) of 31 mu M. The binding of compound 1 to the proposed hydrophobic pocket of gp41 was further validated by site-directed peptide mutagenesis experiments. (C) 2009 Elsevier Ltd. All rights reserved.