methyl 6-[(E)-2-[4-(tert-butoxycarbonylamino)phenyl]ethenylsulfonamido-N-(5-methylhexyl)]hexanoate | 389140-43-6

• 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: methyl 6-[(E)-2-[4-(tert-butoxycarbonylamino)phenyl]ethenylsulfonamido-N-(5-methylhexyl)]hexanoate
• 英文别名: methyl 6-[5-methylhexyl-[(E)-2-[4-[(2-methylpropan-2-yl)oxycarbonylamino]phenyl]ethenyl]sulfonylamino]hexanoate
• CAS: 389140-43-6
• 化学式: C₂₇H₄₄N₂O₆S
• 分子量: 524.722
• InChiKey: GGJIMFVFBDALQT-DYTRJAOYSA-N

物化性质

• 密度：
  1.125±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.5
• 重原子数：
  36
• 可旋转键数：
  18
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.63
• 拓扑面积：
  110
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  methyl 6-[(E)-2-[4-(tert-butoxycarbonylamino)phenyl]ethenylsulfonamido-N-(5-methylhexyl)]hexanoate 、 三氟乙酸 以 氯仿 为溶剂， 反应 0.08h， 以93%的产率得到methyl 6-[(E)-2-(4-aminophenyl)-N-(5-methylhexyl)ethenylsulfonamido]hexanoate trifluoroacetate
  参考文献：
  名称：

  Design and Synthesis of Non-peptidic Inhibitors for the Syk C-Terminal SH2 Domain Based on Structure-Based In-Silico Screening

  摘要：

  Structure-based in-silico screening was carried out for the Syk C-terminal SH2 domain. Fragments that could interact with the pY or pY+1 pockets were selected by our in-silico screening. After tethering two fragments bound to these pockets, we have designed and synthesized new compounds that show favorable interaction with the pY+3 pocket. One such compound, having a cyclohexylmalonic acid moiety identified as a novel potent phosphotyrosyl mimetic, exhibited an affinity comparable to that of the monophosphorylated ligand peptide.

  DOI：

  10.1021/jm010313k
• 作为产物：
  描述：

  6-氨基己酸 在 盐酸 、 potassium carbonate 、 三乙胺 作用下， 以 氯仿 、 N,N-二甲基甲酰胺 为溶剂， 反应 15.25h， 生成 methyl 6-[(E)-2-[4-(tert-butoxycarbonylamino)phenyl]ethenylsulfonamido-N-(5-methylhexyl)]hexanoate
  参考文献：
  名称：

  Design and Synthesis of Non-peptidic Inhibitors for the Syk C-Terminal SH2 Domain Based on Structure-Based In-Silico Screening

  摘要：

  Structure-based in-silico screening was carried out for the Syk C-terminal SH2 domain. Fragments that could interact with the pY or pY+1 pockets were selected by our in-silico screening. After tethering two fragments bound to these pockets, we have designed and synthesized new compounds that show favorable interaction with the pY+3 pocket. One such compound, having a cyclohexylmalonic acid moiety identified as a novel potent phosphotyrosyl mimetic, exhibited an affinity comparable to that of the monophosphorylated ligand peptide.

  DOI：

  10.1021/jm010313k

文献信息

• Design and Synthesis of Non-peptidic Inhibitors for the Syk C-Terminal SH2 Domain Based on Structure-Based In-Silico Screening
  作者：Tatsuya Niimi、Masaya Orita、Miwa Okazawa-Igarashi、Hitoshi Sakashita、Kazumi Kikuchi、Evelyn Ball、Atsushi Ichikawa、Yoko Yamagiwa、Shuichi Sakamoto、Akihiro Tanaka、Shinichi Tsukamoto、Shigeo Fujita、Kuniaki Tatsuta、Yasuhide Maeda、Ken Chikauchi

  DOI：10.1021/jm010313k

  日期：2001.12.1

  Structure-based in-silico screening was carried out for the Syk C-terminal SH2 domain. Fragments that could interact with the pY or pY+1 pockets were selected by our in-silico screening. After tethering two fragments bound to these pockets, we have designed and synthesized new compounds that show favorable interaction with the pY+3 pocket. One such compound, having a cyclohexylmalonic acid moiety identified as a novel potent phosphotyrosyl mimetic, exhibited an affinity comparable to that of the monophosphorylated ligand peptide.