2-(3'-氨基-[1,1'-联苯]-3-基)乙酸甲酯 | 1059678-65-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 中文名称: 2-(3'-氨基-[1,1'-联苯]-3-基)乙酸甲酯
• 英文名称: (3'-amino-biphenyl-3-yl)-acetic acid methyl ester
• 英文别名: (3'-Amino-biphenyl-3-yl)-acetic acid methyl ester；methyl 2-[3-(3-aminophenyl)phenyl]acetate
• CAS: 1059678-65-7
• 化学式: C₁₅H₁₅NO₂
• 分子量: 241.29
• InChiKey: IAAHGDFSVPBOQN-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  18
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  52.3
• 氢给体数：
  1
• 氢受体数：
  3

安全信息

• 海关编码：
  2922499990

反应信息

• 作为反应物：
  描述：

  2-(3'-氨基-[1,1'-联苯]-3-基)乙酸甲酯 在 盐酸 、 草酰氯 、 三乙胺 、 lithium hydroxide 作用下， 以 四氢呋喃 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 26.0h， 生成
  参考文献：
  名称：

  Antibacterial Drug Leads: DNA and Enzyme Multitargeting

  摘要：

  We report the results of an investigation of the activity of a series of amidine and bisamidine compounds against Staphylococcus aureus and Escherichia coli. The most active compounds bound to an AT-rich DNA dodecamer (CGCGAATTCGCG)(2) and using DSC were found to increase the melting transition by up to 24 degrees C. Several compounds also inhibited undecaprenyl diphosphate synthase (UPPS) with IC50 values of 100-500 nM, and we found good correlations (R-2 = 0.89, S. aureus; R-2 = 0.79, E. coli) between experimental and predicted cell growth inhibition by using DNA Delta(Tm) and UPPS IC50 experimental results together with one computed descriptor. We also solved the structures of three bisamidines binding to DNA as well as three UPPS structures. Overall, the results are of general interest in the context of the development of resistance-resistant antibiotics that involve multitargeting.

  DOI：

  10.1021/jm501449u
• 作为产物：
  描述：

  3-氨基苯硼酸 、 2-(3-溴苯基)乙酸甲酯 在 四(三苯基膦)钯 、 sodium carbonate 作用下， 以 乙醇 、 水 、 甲苯 为溶剂， 以56%的产率得到2-(3'-氨基-[1,1'-联苯]-3-基)乙酸甲酯
  参考文献：
  名称：

  Inhibition of Geranylgeranyl Diphosphate Synthase by Bisphosphonates: A Crystallographic and Computational Investigation

  摘要：

  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.

  DOI：

  10.1021/jm800325y

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.
• Antibacterial Drug Leads: DNA and Enzyme Multitargeting
  作者：Wei Zhu、Yang Wang、Kai Li、Jian Gao、Chun-Hsiang Huang、Chun-Chi Chen、Tzu-Ping Ko、Yonghui Zhang、Rey-Ting Guo、Eric Oldfield

  DOI：10.1021/jm501449u

  日期：2015.2.12

  We report the results of an investigation of the activity of a series of amidine and bisamidine compounds against Staphylococcus aureus and Escherichia coli. The most active compounds bound to an AT-rich DNA dodecamer (CGCGAATTCGCG)(2) and using DSC were found to increase the melting transition by up to 24 degrees C. Several compounds also inhibited undecaprenyl diphosphate synthase (UPPS) with IC50 values of 100-500 nM, and we found good correlations (R-2 = 0.89, S. aureus; R-2 = 0.79, E. coli) between experimental and predicted cell growth inhibition by using DNA Delta(Tm) and UPPS IC50 experimental results together with one computed descriptor. We also solved the structures of three bisamidines binding to DNA as well as three UPPS structures. Overall, the results are of general interest in the context of the development of resistance-resistant antibiotics that involve multitargeting.