5'-O-(4,4'-dimethoxytrityl)-2'-O-(tert-butyldimethylsilyl)-N⁶-benzoyl-2-(4-phenylbutyl)adenosine | 504406-67-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: 5'-O-(4,4'-dimethoxytrityl)-2'-O-(tert-butyldimethylsilyl)-N⁶-benzoyl-2-(4-phenylbutyl)adenosine
• 英文别名: N-[9-[(2R,3R,4R,5R)-5-[[bis(4-methoxyphenyl)-phenylmethoxy]methyl]-3-[tert-butyl(dimethyl)silyl]oxy-4-hydroxyoxolan-2-yl]-2-(4-phenylbutyl)purin-6-yl]benzamide
• CAS: 504406-67-1
• 化学式: C₅₄H₆₁N₅O₇Si
• 分子量: 920.193
• InChiKey: NCUYOIJWKBAENN-YQZIWZOKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  10.32
• 重原子数：
  67.0
• 可旋转键数：
  18.0
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  139.08
• 氢给体数：
  2.0
• 氢受体数：
  11.0

反应信息

• 作为反应物：
  描述：

  双(二异丙基氨基)(2-氰基乙氧基)膦 、 5'-O-(4,4'-dimethoxytrityl)-2'-O-(tert-butyldimethylsilyl)-N⁶-benzoyl-2-(4-phenylbutyl)adenosine 在 N-甲基咪唑 、 2,3,5-三甲基吡啶 作用下， 以 四氢呋喃 为溶剂， 以69%的产率得到5'-O-(4,4'-dimethoxytrityl)-2'-O-(tert-butyldimethylsilyl)-N⁶-benzoyl-2-(4-phenylbutyl)adenosine 3'-N,N-disopropyl(cyanoethyl)phosphoramidite
  参考文献：
  名称：

  Design of an Adenosine Analogue that Selectively Improves the Affinity of a Mutant U1A Protein for RNA

  摘要：

  The RNA recognition motif (RRM), one of the most common RNA binding domains, contains three highly conserved aromatic amino acids that participate in stacking interactions with RNA bases. We have investigated the contribution of these highly conserved aromatic amino acids to the affinity of the complex formed between the N-terminal RRM of the U1A protein and stem loop 2 of U1 snRNA. Previously, we found that substitution of one of these conserved aromatic amino acids, Phe56, with Ala resulted in a large destabilization of the complex. Here, we have modified A6, the base in stem loop 2 RNA that stacks with Phe56, to compensate for a portion of the destabilization caused by the Phe56Ala mutation. We have designed two modified adenosines, A-3CPh and A-4CPh, in which a phenyl group is linked to the adenosine such that it may replace the phenyl group that is eliminated by the Phe56Ala mutation in the complex. We have found that incorporation of A-3CPh into stem loop 2 RNA stabilizes the complex formed with Phe56Ala by 0.6 kcal/mol, while incorporation of A-4CPh into stem loop 2 RNA stabilizes this complex by 1.8 kcal/mol. Either base modification destabilizes the wild-type complex by 0.8-0.9 kcal/mol. Experiments with other U1 A mutant proteins suggest that the stabilization of the complex between the Phe56Ala U1 A protein and stem loop 2 RNA is due to a specific interaction between the Phe56Ala U1A protein and A6-4CPh stem loop 2 RNA.

  DOI：

  10.1021/ja021267w
• 作为产物：
  描述：

  2-(4-phenyl-1-butyn-1-yl)adenosine 在 10 percent Pd/C 吡啶 、 三甲基氯硅烷 、 18-冠醚-6 、 氢气 、 potassium hydride 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 4.33h， 生成 5'-O-(4,4'-dimethoxytrityl)-2'-O-(tert-butyldimethylsilyl)-N⁶-benzoyl-2-(4-phenylbutyl)adenosine
  参考文献：
  名称：

  Design of an Adenosine Analogue that Selectively Improves the Affinity of a Mutant U1A Protein for RNA

  摘要：

  The RNA recognition motif (RRM), one of the most common RNA binding domains, contains three highly conserved aromatic amino acids that participate in stacking interactions with RNA bases. We have investigated the contribution of these highly conserved aromatic amino acids to the affinity of the complex formed between the N-terminal RRM of the U1A protein and stem loop 2 of U1 snRNA. Previously, we found that substitution of one of these conserved aromatic amino acids, Phe56, with Ala resulted in a large destabilization of the complex. Here, we have modified A6, the base in stem loop 2 RNA that stacks with Phe56, to compensate for a portion of the destabilization caused by the Phe56Ala mutation. We have designed two modified adenosines, A-3CPh and A-4CPh, in which a phenyl group is linked to the adenosine such that it may replace the phenyl group that is eliminated by the Phe56Ala mutation in the complex. We have found that incorporation of A-3CPh into stem loop 2 RNA stabilizes the complex formed with Phe56Ala by 0.6 kcal/mol, while incorporation of A-4CPh into stem loop 2 RNA stabilizes this complex by 1.8 kcal/mol. Either base modification destabilizes the wild-type complex by 0.8-0.9 kcal/mol. Experiments with other U1 A mutant proteins suggest that the stabilization of the complex between the Phe56Ala U1 A protein and stem loop 2 RNA is due to a specific interaction between the Phe56Ala U1A protein and A6-4CPh stem loop 2 RNA.

  DOI：

  10.1021/ja021267w