| 941579-10-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• CAS: 941579-10-8
• 化学式: C₂₅H₂₆O₅
• 分子量: 406.478
• InChiKey: LPFIOFGNZANZLV-GOSISDBHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.73
• 重原子数：
  30.0
• 可旋转键数：
  9.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.24
• 拓扑面积：
  64.99
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  、 氯乙腈 在 三乙胺 作用下， 反应 3.0h， 以76%的产率得到
  参考文献：
  名称：

  Unexpected Preference of the E. coli Translation System for the Ester Bond during Incorporation of Backbone-Elongated Substrates

  摘要：

  There have been recent advances in the ribosomal synthesis of various molecules composed of nonnatural ribosomal substrates. However, the ribosome has strict limitations on substrates with elongated backbones. Here, we show an unexpected loophole in the E. coli translation system, based on a remarkable disparity in its selectivity for beta-amino/hydroxy acids. We challenged beta-hydroxypropionic acid (beta-HPA), which is less nucleophilic than beta-amino acids but free from protonation, to produce a new repertoire of ribosome-compatible but main-chain-elongated substrates. PAGE analysis and mass-coupled S-tag assays of amber suppression experiments using yeast suppressor tRNA(CUA)(Phe) confirmed the actual incorporation of beta-HPA into proteins/oligopeptides. We investigated the side-chain effects of beta-HPA and found that the side chain at position alpha and R stereochemistry of the beta-substrate is preferred and even notably enhances the efficiency of incorporation as compared to the parent substrate. These results indicate that the E. coli translation machinery can utilize main-chain-elongated substrates if the pK(a) of the substrate is appropriately chosen.

  DOI：

  10.1021/ja068033n
• 作为产物：
  描述：

  (R)-3-[Bis-(4-methoxy-phenyl)-phenyl-methoxy]-2-methyl-propionic acid methyl ester 在 lithium hydroxide 作用下， 以103 mg的产率得到
  参考文献：
  名称：

  Unexpected Preference of the E. coli Translation System for the Ester Bond during Incorporation of Backbone-Elongated Substrates

  摘要：

  There have been recent advances in the ribosomal synthesis of various molecules composed of nonnatural ribosomal substrates. However, the ribosome has strict limitations on substrates with elongated backbones. Here, we show an unexpected loophole in the E. coli translation system, based on a remarkable disparity in its selectivity for beta-amino/hydroxy acids. We challenged beta-hydroxypropionic acid (beta-HPA), which is less nucleophilic than beta-amino acids but free from protonation, to produce a new repertoire of ribosome-compatible but main-chain-elongated substrates. PAGE analysis and mass-coupled S-tag assays of amber suppression experiments using yeast suppressor tRNA(CUA)(Phe) confirmed the actual incorporation of beta-HPA into proteins/oligopeptides. We investigated the side-chain effects of beta-HPA and found that the side chain at position alpha and R stereochemistry of the beta-substrate is preferred and even notably enhances the efficiency of incorporation as compared to the parent substrate. These results indicate that the E. coli translation machinery can utilize main-chain-elongated substrates if the pK(a) of the substrate is appropriately chosen.

  DOI：

  10.1021/ja068033n