[4-[[4-[[(2S)-1-[[(2S)-1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-oxobutanoyl]amino]phenyl] butanoate | 1377324-51-0

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: [4-[[4-[[(2S)-1-[[(2S)-1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-oxobutanoyl]amino]phenyl] butanoate
• CAS: 1377324-51-0
• 化学式: C₃₂H₃₆N₄O₈
• 分子量: 604.66
• InChiKey: JBJWEHPIYZOTDZ-SVBPBHIXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  44
• 可旋转键数：
  16
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.28
• 拓扑面积：
  197
• 氢给体数：
  6
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  ethyl 4-aminophenyl acetate 在 哌啶 、 rink amide MBHA resin 、 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 5.0h， 生成 [4-[[4-[[(2S)-1-[[(2S)-1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-oxobutanoyl]amino]phenyl] butanoate
  参考文献：
  名称：

  An approach for differentiating isozymes. Construction of libraries containing short aromatic peptides as part of a method to design selective inhibitors against lipases

  摘要：

  Through synthesis and assays of peptidyl substrates, we could select substrates having peptidyl complementary against lipases. The best substrate showed 20-fold improved K-m relative to non-peptidyl substrate. Using this information, we generated selective inhibitors. Lipase activities with peptidyl substrates were represented as fingerprints. Differences in fingerprints reflect different structures near active site of lipases, could be used for generating selective inhibitors. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2012.03.048

文献信息

• An approach for differentiating isozymes. Construction of libraries containing short aromatic peptides as part of a method to design selective inhibitors against lipases
  作者：Sangeun Park、Jaehoon Yu

  DOI：10.1016/j.bmcl.2012.03.048

  日期：2012.5

  Through synthesis and assays of peptidyl substrates, we could select substrates having peptidyl complementary against lipases. The best substrate showed 20-fold improved K-m relative to non-peptidyl substrate. Using this information, we generated selective inhibitors. Lipase activities with peptidyl substrates were represented as fingerprints. Differences in fingerprints reflect different structures near active site of lipases, could be used for generating selective inhibitors. (C) 2012 Elsevier Ltd. All rights reserved.