6,6'-(2,1-亚苯基)二(1,3,5-三嗪-2,4-二胺) | 5118-79-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 三嗪类
• 中文名称: 6,6'-(2,1-亚苯基)二(1,3,5-三嗪-2,4-二胺)
• 英文名称: 6-[2-(4,6-diamino-1,3,5-triazin-2-yl)phenyl]-1,3,5-triazine-2,4-diamine
• 英文别名: 1,2-bis(2,4-diamino-1,3,5-triazin-6-yl)benzene；NCI-4429；6,6'-o-phenylene-bis-[1,3,5]triazine-2,4-diamine；6,6'-o-phenylene-bis-[1,3,5]triazine-2,4-diyldiamine；6,6'-o-Phenylen-bis-[1,3,5]triazin-2,4-diyldiamin；o-Phtaloguanamin；s-Triazine, 2,2'-O-phenylene-bis(4,6-diamino-
• CAS: 5118-79-6
• 化学式: C₁₂H₁₂N₁₀
• mdl: MFCD01871199
• 分子量: 296.294
• InChiKey: FNNFAYGKUXMHSH-UHFFFAOYSA-N

物化性质

• 熔点：
  359 °C
• 沸点：
  834.1±75.0 °C(Predicted)
• 密度：
  1.572±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  22
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  181
• 氢给体数：
  4
• 氢受体数：
  10

安全信息

• 海关编码：
  2933699090

反应信息

• 作为产物：
  描述：

  二聚氰胺 、 1,2-二氰基苯 在 氢氧化钾 作用下， 以 二甲基亚砜 为溶剂， 反应 0.17h， 以80%的产率得到6,6'-(2,1-亚苯基)二(1,3,5-三嗪-2,4-二胺)
  参考文献：
  名称：

  Green synthesis and self-association of 2,4-diamino-1,3,5-triazine derivatives

  摘要：

  2,4-二氨基-1,3,5-三嗪是通过在微波照射下将二氰胺与腈类反应制备的，这种方法可以被视为一种绿色程序，因为在合成和纯化过程中减少了溶剂的使用，反应时间短且过程简单。通过NMR光谱在溶液中确认了其结构。可变温度实验用于计算关于氨基-三嗪键旋转的活化自由能。三种2,4-二氨基-6-R-1,3,5-三嗪衍生物（3a: R=苯基, 3i: R=1-哌啶基和3g: R=1-苯基吡唑-3-基）的晶体结构已通过X射线分析确定。N–H⋯N相互作用因结构的不同而变化，导致从伪蜂窝网络到波纹玫瑰层的变化。

  DOI：

  10.1039/b315956f

文献信息

• US2684366
  申请人：——

  公开号：——

  公开（公告）日：——
• LIGANDS THAT TARGET HEPATITIS C VIRUS E2 PROTEIN
  申请人：BALHORN Rodney

  公开号：US20160361311A1

  公开（公告）日：2016-12-15

  Hepatitis C Virus (HCV) infects 200 million individuals worldwide. Although several FDA approved drugs targeting the HCV serine protease and polymerase have shown promising results, there is a need for better drugs that are effective in treating a broader range of HCV genotypes and subtypes without being used in combination with interferon and/or ribavirin. Recently, the crystal structure of the core of the HCV E2 protein (E2c) has been determined, providing structural information that can now be used to target the E2 protein and develop drugs that disrupt the early stages of HCV infection by blocking E2's interaction with different host factors. By targeting sites containing conserved E2 amino acids in the CD81 binding site on HCV E2, one might also be able to develop drugs that block HCV infection in a genotype-independent manner. Using the E2c structure as a template, a structural model of the E2 protein core (residues 421-645) was developed that includes the three amino acid segments that are not present in the E2c crystal structure. Blind docking of a diverse library of 1715 small molecules to this model led to the identification of a set of 34 ligands predicted to bind near conserved amino acid residues involved in the HCV E2:CD81 interaction. Surface plasmon resonance was used to screen the ligand set for binding to recombinant E2 protein, and the best binders were subsequently tested to identify compounds that inhibit the infection of hepatocytes by HCV. One compound, 281816, blocked E2 binding to CD81 and inhibited hepatocyte infection by HCV genotypes 1a, 1b, 2a, 2b, 4a and 6a with IC50's ranging from 2.2 μM to 4.6 μM. Methods are described for preventing or treating HCV infection using small molecule inhibitors such as 281816 that target E2 and disrupt its interactions.
• [EN] LIGANDS THAT TARGET HEPATITIS C VIRUS E2 PROTEIN<br/>[FR] LIGANDS CIBLANT LA PROTÉINE E2 DU VIRUS DE L'HÉPATITE C
  申请人：AMERICAN UNIVERSITY OF CAIRO AUC

  公开号：WO2015128744A2

  公开（公告）日：2015-09-03

  Hepatitis C Virus (HCV) infects 200 million individuals worldwide. Although several FDA approved drugs targeting the HCV serine protease and polymerase have shown promising results, there is a need for better drugs that are effective in treating a broader range of HCV genotypes and subtypes without being used in combination with interferon and/or ribavirin. Recently, the crystal structure of the core of the HCV E2 protein (E2c) has been determined, providing structural information that can now be used to target the E2 protein and develop drugs that disrupt the early stages of HCV infection by blocking E2's interaction with different host factors. By targeting sites containing conserved E2 amino acids in the CD81 binding site on HCV E2, one might also be able to develop drugs that block HCV infection in a genotype-independent manner. Using the E2c structure as a template, a structural model of the E2 protein core (residues 421-645) was developed that includes the three amino acid segments that are not present in the E2c crystal structure. Blind docking of a diverse library of 1715 small molecules to this model led to the identification of a set of 34 ligands predicted to bind near conserved amino acid residues involved in the HCV E2: CD81 interaction. Surface plasmon resonance was used to screen the ligand set for binding to recombinant E2 protein, and the best binders were subsequently tested to identify compounds that inhibit the infection of hepatocytes by HCV. One compound, 281816, blocked E2 binding to CD81 and inhibited hepatocyte infection by HCV genotypes la, lb, 2a, 2b, 4a and 6a with IC50's ranging from 2.2 μΜ to 4.6 μΜ. Methods are described for preventing or treating HCV infection using small molecule inhibitors such as 281816 that target E2 and disrupt its interactions.