(E)-5,5-bis[(phenylmethoxy)methyl]-3-[5-methyl-3-(2-methylpropyl)hexylidene]-4,5-dihydrofuran-2-thione | 862549-45-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (E)-5,5-bis[(phenylmethoxy)methyl]-3-[5-methyl-3-(2-methylpropyl)hexylidene]-4,5-dihydrofuran-2-thione
• 英文别名: (3E)-3-[5-methyl-3-(2-methylpropyl)hexylidene]-5,5-bis(phenylmethoxymethyl)oxolane-2-thione
• CAS: 862549-45-9
• 化学式: C₃₁H₄₂O₃S
• 分子量: 494.739
• InChiKey: DAHPOPZVFJSTTI-MUFRIFMGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.1
• 重原子数：
  35
• 可旋转键数：
  14
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  59.8
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (E)-5,5-bis[(phenylmethoxy)methyl]-3-[5-methyl-3-(2-methylpropyl)hexylidene]-4,5-dihydrofuran-2-thione 在 三溴化硼 作用下， 以 二氯甲烷 为溶剂， 反应 0.5h， 以81%的产率得到5,5-Bis-hydroxymethyl-3-[3-isobutyl-5-methyl-hex-(E)-ylidene]-dihydro-furan-2-thione
  参考文献：
  名称：

  Conformationally Constrained Analogues of Diacylglycerol (DAG). 25. Exploration of the sn-1 and sn-2 Carbonyl Functionality Reveals the Essential Role of the sn-1 Carbonyl at the Lipid Interface in the Binding of DAG-Lactones to Protein Kinase C

  摘要：

  Diacylglycerol (DAG) lactones with altered functionality (C=O -> CH2 or C=O -> C=S) at the sn-1 and sn-2 carbonyl pharmacophores were synthesized and used as probes to dissect the individual role of each carbonyl in the binding to protein kinase C (PKC). The results suggest that the hydrated sn-1 carbonyl is engaged in very strong hydrogen-bonding interactions with the charged lipid headgroups and organized water molecules at the lipid interface. Conversely, the sn-2 carbonyl has a more modest contribution to the binding process as a result of its involvement with the receptor (Cl domain) via conventional hydrogen bonding to the protein. The parent DAG-lactones, E-6 and Z-7, were designed to bind exclusively in the sn-2 binding mode to ensure the correct orientation and disposition of pharmacophores at the binding site.

  DOI：

  10.1021/jm050352m
• 作为产物：
  描述：

  二异丁基酮 在 palladium on activated charcoal 劳森试剂 、 4 A molecular sieve 、 氢气 、 甲基磺酰氯 、 三乙胺 、 pyridinium chlorochromate 、 lithium hexamethyldisilazane 作用下， 以 四氢呋喃 、 二氯甲烷 、 甲苯 为溶剂， 反应 46.75h， 生成 (E)-5,5-bis[(phenylmethoxy)methyl]-3-[5-methyl-3-(2-methylpropyl)hexylidene]-4,5-dihydrofuran-2-thione
  参考文献：
  名称：

  Conformationally Constrained Analogues of Diacylglycerol (DAG). 25. Exploration of the sn-1 and sn-2 Carbonyl Functionality Reveals the Essential Role of the sn-1 Carbonyl at the Lipid Interface in the Binding of DAG-Lactones to Protein Kinase C

  摘要：

  Diacylglycerol (DAG) lactones with altered functionality (C=O -> CH2 or C=O -> C=S) at the sn-1 and sn-2 carbonyl pharmacophores were synthesized and used as probes to dissect the individual role of each carbonyl in the binding to protein kinase C (PKC). The results suggest that the hydrated sn-1 carbonyl is engaged in very strong hydrogen-bonding interactions with the charged lipid headgroups and organized water molecules at the lipid interface. Conversely, the sn-2 carbonyl has a more modest contribution to the binding process as a result of its involvement with the receptor (Cl domain) via conventional hydrogen bonding to the protein. The parent DAG-lactones, E-6 and Z-7, were designed to bind exclusively in the sn-2 binding mode to ensure the correct orientation and disposition of pharmacophores at the binding site.

  DOI：

  10.1021/jm050352m

文献信息

• Conformationally Constrained Analogues of Diacylglycerol (DAG). 25. Exploration of the <i>sn</i>-1 and <i>sn</i>-2 Carbonyl Functionality Reveals the Essential Role of the <i>sn</i>-1 Carbonyl at the Lipid Interface in the Binding of DAG-Lactones to Protein Kinase C
  作者：Ji-Hye Kang、Megan L. Peach、Yongmei Pu、Nancy E. Lewin、Marc C. Nicklaus、Peter M. Blumberg、Victor E. Marquez

  DOI：10.1021/jm050352m

  日期：2005.9.1

  Diacylglycerol (DAG) lactones with altered functionality (C=O -> CH2 or C=O -> C=S) at the sn-1 and sn-2 carbonyl pharmacophores were synthesized and used as probes to dissect the individual role of each carbonyl in the binding to protein kinase C (PKC). The results suggest that the hydrated sn-1 carbonyl is engaged in very strong hydrogen-bonding interactions with the charged lipid headgroups and organized water molecules at the lipid interface. Conversely, the sn-2 carbonyl has a more modest contribution to the binding process as a result of its involvement with the receptor (Cl domain) via conventional hydrogen bonding to the protein. The parent DAG-lactones, E-6 and Z-7, were designed to bind exclusively in the sn-2 binding mode to ensure the correct orientation and disposition of pharmacophores at the binding site.