| 1597428-96-0

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 二芳基庚烷
• CAS: 1597428-96-0
• 化学式: C₅₁H₇₀O₉Si
• 分子量: 855.197
• InChiKey: DGONJTBXRYWMTG-QSWGGJQDSA-N

反应信息

• 作为反应物：
  描述：

  在 四丁基氟化铵 作用下， 以 四氢呋喃 为溶剂， 生成 ditert-butyl 2-[3-[(E)-[5-(hydroxymethyl)-5-[[5-methyl-3-(2-methylpropyl)hexanoyl]oxymethyl]-2-oxooxolan-3-ylidene]methyl]phenyl]propanedioate
  参考文献：
  名称：

  Diacylglycerol Lactones Targeting the Structural Features That Distinguish the Atypical C1 Domains of Protein Kinase C ζ and ι from Typical C1 Domains

  摘要：

  To explore the feasibility of developing ligands targeted to the atypical C1 domains of protein kinase C zeta and iota, we have prepared diacylglycerol lactones substituted with hydrophilic groups on their side chains, which potentially could interact with the arginine residues that distinguish the atypical C1 domains of PKC zeta and PKC?iota from typical C1 domains, and we have measured their binding to mutated versions of the C1b domain of PKC delta that incorporate one or more of these arginine residues. The most selective of the diacylglycerol lactones showed only a 10-fold reduction in binding affinity with the triple arginine mutant (N7R/S10R/L20R) compared to the wild-type, whereas phorbol 12,13-dibutyrate showed a 6000-fold loss of affinity. Molecular modeling confirms that these ligands are indeed able to interact with the arginine residues. Our results show that dramatic changes in selectivity can be obtained through appropriate substitution of diacylglycerol lactones.

  DOI：

  10.1021/jm500165n
• 作为产物：
  描述：

  在 4-二甲氨基吡啶 、 ammonium cerium (IV) nitrate 、 三乙胺 、 lithium hexamethyldisilazane 作用下， 以 四氢呋喃 、 二氯甲烷 、 水 、 乙腈 为溶剂， 反应 1.0h， 生成
  参考文献：
  名称：

  Diacylglycerol Lactones Targeting the Structural Features That Distinguish the Atypical C1 Domains of Protein Kinase C ζ and ι from Typical C1 Domains

  摘要：

  To explore the feasibility of developing ligands targeted to the atypical C1 domains of protein kinase C zeta and iota, we have prepared diacylglycerol lactones substituted with hydrophilic groups on their side chains, which potentially could interact with the arginine residues that distinguish the atypical C1 domains of PKC zeta and PKC?iota from typical C1 domains, and we have measured their binding to mutated versions of the C1b domain of PKC delta that incorporate one or more of these arginine residues. The most selective of the diacylglycerol lactones showed only a 10-fold reduction in binding affinity with the triple arginine mutant (N7R/S10R/L20R) compared to the wild-type, whereas phorbol 12,13-dibutyrate showed a 6000-fold loss of affinity. Molecular modeling confirms that these ligands are indeed able to interact with the arginine residues. Our results show that dramatic changes in selectivity can be obtained through appropriate substitution of diacylglycerol lactones.

  DOI：

  10.1021/jm500165n