Fmoc-Leu-Leu-OBzl | 1013661-54-5

• 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: Fmoc-Leu-Leu-OBzl
• 英文别名: benzyl (2S)-2-[[(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-methylpentanoyl]amino]-4-methylpentanoate
• CAS: 1013661-54-5
• 化学式: C₃₄H₄₀N₂O₅
• 分子量: 556.702
• InChiKey: OVEGDGNSSJMTLH-CONSDPRKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.3
• 重原子数：
  41
• 可旋转键数：
  14
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  93.7
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  Fmoc-Leu-Leu-OBzl 在 palladium 10% on activated carbon 、 氢气 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 以86%的产率得到Fmoc-L-亮氨酰-亮氨酸
  参考文献：
  名称：

  Glycopeptide probes for understanding peptide specificity of the folding sensor enzyme UGGT

  摘要：

  A systematic series of chitobiose-modified pentapeptides with sequence variations of hydrophobic leucine and hydrophilic serine were synthesized. The resulting glycopeptides were used as molecular probes to elucidate aglycon peptide specificity of the glycoprotein-folding sensor enzyme UGGT. Inhibitory experiments with a synthetic fluorescent glyco-substrate and the glycopeptides revealed that UGGT prefers a serine residue directly linked to C-terminal of the N-glycosylation site in its substrate recognition. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2014.11.013
• 作为产物：
  描述：

  L-亮氨酸苄基酯 、 Fmoc-L-亮氨酸 在 1-丙基磷酸酐 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 为溶剂， 以> 99 %的产率得到Fmoc-Leu-Leu-OBzl
  参考文献：
  名称：

  由仿生环丙基膦酸酐 (T3P®) 介导的快速溶液相和液相肽合成（SolPSS 和 LPPS）

  摘要：

  基于肽的疗法的应用不断增长，需要从工业规模扩大的角度开发有效的方案。T3P®（环丙基膦酸酐）通过仿生方法促进溶液相中的酰胺化，类似于代谢途径中 ATP 抓取酶催化的羧基部分的激活。T3P® 诱导偶联反应在本研究中应用于溶液相肽合成 (SolPPS)。肽键形成在几分钟内发生，效率高且无差向异构化，产生水溶性副产物，均使用 N-Boc 或 N-Fmoc 氨基酸。优化的方案已成功应用于五肽的迭代合成，还可以减少溶剂体积，从而提高工艺的可持续性。该方案最终扩展到液相肽合成（LPPS），其中使用沉淀进行肽的分离，从而也表明了这种偶联试剂对这种新兴技术的适用性。

  DOI：

  10.3390/molecules28207183

文献信息

• BENZYLIC COMPOUND
  申请人：TAKAHASHI Daisuke

  公开号：US20110160433A1

  公开（公告）日：2011-06-30

  The present invention provides a protecting reagent that can be removed in a high yield even under acidic conditions and can afford a resulting product at a high purity in an organic synthesis reaction such as peptide synthesis and the like. The inventive protecting reagent is particular benzylic compound having only one hydroxyl group substituted by an organic group having an aliphatic hydrocarbon group having a carbon number of not less than 14.

  本发明提供了一种保护试剂，即使在酸性条件下也可以高收率地去除，并且可以在有机合成反应中（如肽合成等）得到高纯度的产物。该发明的保护试剂是一种特定的苄基化合物，仅有一个羟基被具有不少于14个碳原子的脂肪烃基的有机基取代。
• Benzylic compound
  申请人：Takahashi Daisuke

  公开号：US08859732B2

  公开（公告）日：2014-10-14

  The present invention provides a protecting reagent that can be removed in a high yield even under acidic conditions and can afford a resulting product at a high purity in an organic synthesis reaction such as peptide synthesis and the like. The inventive protecting reagent is particular benzylic compound having only one hydroxyl group substituted by an organic group having an aliphatic hydrocarbon group having a carbon number of not less than 14.

  本发明提供了一种保护试剂，即使在酸性条件下也能高收率地去除，并且在有机合成反应中，如肽合成等反应中能够提供高纯度的产物。本发明的保护试剂是一种苯甲基化合物，仅有一个羟基被具有不少于14个碳原子的脂肪烃基的有机基取代。
• Unusual Sculpting of Dipeptide Particles by Ultrasound Induces Gelation
  作者：David Bardelang、Franck Camerel、James C. Margeson、Donald M. Leek、Marc Schmutz、Md. Badruz Zaman、Kui Yu、Dmitriy V. Soldatov、Raymond Ziessel、Christopher I. Ratcliffe、John A. Ripmeester

  DOI：10.1021/ja711342y

  日期：2008.3.1

  A readily synthesized dipeptide shows unprecedented gelation behavior when dispersed and submitted to ultrasound in nonsolvents. SEM and FFEM revealed spectacular shape changes from a sheet-like material into a highly interconnected fiber network and ribbons while the dipeptide maintains an anti conformation inside beta-sheets at the molecular scale.
• Glycopeptide probes for understanding peptide specificity of the folding sensor enzyme UGGT
  作者：Takaya Kudo、Makoto Hirano、Toshihiro Ishihara、Shun Shimura、Kiichiro Totani

  DOI：10.1016/j.bmcl.2014.11.013

  日期：2014.12

  A systematic series of chitobiose-modified pentapeptides with sequence variations of hydrophobic leucine and hydrophilic serine were synthesized. The resulting glycopeptides were used as molecular probes to elucidate aglycon peptide specificity of the glycoprotein-folding sensor enzyme UGGT. Inhibitory experiments with a synthetic fluorescent glyco-substrate and the glycopeptides revealed that UGGT prefers a serine residue directly linked to C-terminal of the N-glycosylation site in its substrate recognition. (C) 2014 Elsevier Ltd. All rights reserved.