methyl 3,5-bis((dimethylcarbamoyl)thio)-2-naphthoate | 1430800-68-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: methyl 3,5-bis((dimethylcarbamoyl)thio)-2-naphthoate
• CAS: 1430800-68-2
• 化学式: C₁₈H₂₀N₂O₄S₂
• 分子量: 392.5
• InChiKey: BSDFBFNJWGMJMR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.17
• 重原子数：
  26.0
• 可旋转键数：
  3.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.28
• 拓扑面积：
  66.92
• 氢给体数：
  0.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  methyl 3,5-bis((dimethylcarbamoyl)thio)-2-naphthoate 在 sodium hydroxide 、 盐酸 作用下， 以 水 为溶剂， 反应 10.2h， 以83%的产率得到3,5-dimercapto-2-naphthoic acid
  参考文献：
  名称：

  A Synthetic Receptor for Asymmetric Dimethyl Arginine

  摘要：

  Dynamic combinatorial chemistry was utilized to identify a novel small molecule receptor, A(2)D, for asymmetric dimethyl arginine (aRMe(2)), which is a post-translational modification (PTM) in proteins. It is known to play a role in a number of diseases, including spinal muscular atrophy, leukemia, lymphoma, and breast cancer. The receptor exhibits 2.5-7.5-fold selectivity over the isomeric symmetric dimethyl arginine, depending on the surrounding sequence, with binding affinities in the low micromolar range. The affinity and selectivity of A(2)D for the different methylated states of Arg parallels that of proteins that bind to these PTMs. Characterization of the receptor-PTM complex indicates that cation-pi interactions provide the main driving force for binding, loosely mimicking the binding mode found in the recognition of dimethyl arginine by native protein receptors.

  DOI：

  10.1021/ja307907p
• 作为产物：
  描述：

  甲基3,5-二羟基-2-萘酯 在 三乙烯二胺 作用下， 以 二苯醚 、 N,N-二甲基甲酰胺 为溶剂， 反应 29.2h， 生成 methyl 3,5-bis((dimethylcarbamoyl)thio)-2-naphthoate
  参考文献：
  名称：

  A Synthetic Receptor for Asymmetric Dimethyl Arginine

  摘要：

  Dynamic combinatorial chemistry was utilized to identify a novel small molecule receptor, A(2)D, for asymmetric dimethyl arginine (aRMe(2)), which is a post-translational modification (PTM) in proteins. It is known to play a role in a number of diseases, including spinal muscular atrophy, leukemia, lymphoma, and breast cancer. The receptor exhibits 2.5-7.5-fold selectivity over the isomeric symmetric dimethyl arginine, depending on the surrounding sequence, with binding affinities in the low micromolar range. The affinity and selectivity of A(2)D for the different methylated states of Arg parallels that of proteins that bind to these PTMs. Characterization of the receptor-PTM complex indicates that cation-pi interactions provide the main driving force for binding, loosely mimicking the binding mode found in the recognition of dimethyl arginine by native protein receptors.

  DOI：

  10.1021/ja307907p