methyl (2S)-3-methyl-2-[(2-methyl-1-phenylpropyl)amino]butanoate

• 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: methyl (2S)-3-methyl-2-[(2-methyl-1-phenylpropyl)amino]butanoate
• 化学式: C₈H₁₆N₃O₂Pol
• 分子量: 263.37
• InChiKey: BHEOMADTPRUBGS-LOACHALJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  19
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  38.3
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  methyl (2S)-3-methyl-2-[(2-methyl-1-phenylpropyl)amino]butanoate 、 在 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 、 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 3.0h， 生成 C₁₈H₂₈N₄O₇PPol
  参考文献：
  名称：

  Fluorogenic Peptide Substrates for Serine and Threonine Phosphatases

  摘要：

  A new fluorescent assay for Ser/Thr protein phosphatases has been developed. Hydrolysis of a phosphoSer residue liberates the Ser hydroxyl group, which induces a cyclization reaction on the N-terminal carbamate and releases a fluorescent reporter. Sequence selectivity is observed using several peptide substrates against alkaline phosphatase (ALP), bacteriophage lambda protein phosphatase (lambda-PPase), and vaccinia H1 related phosphatase (VHR). These studies suggest that the assay could be a useful tool for profiling the substrate specificities of medicinally important phosphatases.

  DOI：

  10.1021/ol1003065
• 作为产物：
  描述：

  Fmoc-L-缬氨酸 、 在 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium 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 2.0h， 生成 methyl (2S)-3-methyl-2-[(2-methyl-1-phenylpropyl)amino]butanoate
  参考文献：
  名称：

  Selective Disruption of Early/Recycling Endosomes: Release of Disulfide-Linked Cargo Mediated by a N-Alkyl-3β-Cholesterylamine-Capped Peptide

  摘要：

  The use of endocytic uptake pathways to deliver poorly permeable molecules into mammalian cells is often plagued by entrapment and degradation of material in late endosomes and lysosomes. As a strategy to prevent the exposure of cargo to these highly hydrolytic membrane-sealed compartments, we synthesized derivatives of the membrane anchor N-alkyl-3 beta-cholesterylamine that selectively target linked compounds to less hydrolytic early/recycling endosomes. By targeting a pH-dependent membrane-lytic dodecapeptide and dislufide-linked flurophore to these compartments in Chinese hamster ovary cells or Jurkat lymphocytes, membranes of early-recycling endosomes were selectively disrupted, resulting in cleavage of the disulphide and escape of the fluorophore into cytosol and nucleus with low toxicity. The ability os appropriately designed N-alkyl-3 beta-cholesterylamines to deliver cargo into and release dislufide-linked cargo from relatively nonhydrolytic early/recycling endosomes may be useful for the delivery of a variety of sensitive molecules into living mammalian cells.

  DOI：

  10.1021/ja803380a

文献信息

• Indium–Silver- and Zinc–Silver-Mediated Barbier–Grignard-Type Alkylation Reactions of Imines by Using Unactivated Alkyl Halides in Aqueous Media
  作者：Zhi-Liang Shen、Hao-Lun Cheong、Teck-Peng Loh

  DOI：10.1002/chem.200701468

  日期：2008.2.18

  efficient and practical method for the Barbier-Grignard-type alkylation reactions of simple imines by using a one-pot condensation of various aldehydes, amines (including the aliphatic and chiral version), and secondary alkyl iodides has been developed. The reaction proceeded more efficiently in water than in organic solvents. Without the use of CuI, it mainly gave the imine self-reductive coupling product

  在In或Zn / AgI / InCl（3）存在的情况下，通过使用一锅缩合的各种醛，胺（包括脂肪族和手性化合物）的简单亚胺进行Barbier-Grignard型烷基化反应的高效实用方法版本），并且已经开发了仲烷基碘。该反应在水中比在有机溶剂中更有效地进行。不使用CuI，它主要得到亚胺自还原偶联产物，它不是烷基化产物。当使用L-缬氨酸甲酯作为底物时，获得了良好的非对映选择性（高达92：8 dr）。
• Indium (Zinc)−Copper-Mediated Barbier-Type Alkylation Reaction of Nitrones in Water: Synthesis of Amines and Hydroxylamines
  作者：Yong-Sheng Yang、Zhi-Liang Shen、Teck-Peng Loh

  DOI：10.1021/ol8027362

  日期：2009.3.19

  An efficient method for the Barbier-type alkylation reaction of various nitrones (including chiral version) and alkyl halides in water is described. The amines and hydroxylamines can be obtained in good yields, depending on the judicious choice of the metal complexes used.
• Selective Disruption of Early/Recycling Endosomes: Release of Disulfide-Linked Cargo Mediated by a <i>N</i>-Alkyl-3β-Cholesterylamine-Capped Peptide
  作者：Qi Sun、Sutang Cai、Blake R. Peterson

  DOI：10.1021/ja803380a

  日期：2008.8.1

  The use of endocytic uptake pathways to deliver poorly permeable molecules into mammalian cells is often plagued by entrapment and degradation of material in late endosomes and lysosomes. As a strategy to prevent the exposure of cargo to these highly hydrolytic membrane-sealed compartments, we synthesized derivatives of the membrane anchor N-alkyl-3 beta-cholesterylamine that selectively target linked compounds to less hydrolytic early/recycling endosomes. By targeting a pH-dependent membrane-lytic dodecapeptide and dislufide-linked flurophore to these compartments in Chinese hamster ovary cells or Jurkat lymphocytes, membranes of early-recycling endosomes were selectively disrupted, resulting in cleavage of the disulphide and escape of the fluorophore into cytosol and nucleus with low toxicity. The ability os appropriately designed N-alkyl-3 beta-cholesterylamines to deliver cargo into and release dislufide-linked cargo from relatively nonhydrolytic early/recycling endosomes may be useful for the delivery of a variety of sensitive molecules into living mammalian cells.
• Fluorogenic Peptide Substrates for Serine and Threonine Phosphatases
  作者：Fengtian Xue、Christopher T. Seto

  DOI：10.1021/ol1003065

  日期：2010.5.7

  A new fluorescent assay for Ser/Thr protein phosphatases has been developed. Hydrolysis of a phosphoSer residue liberates the Ser hydroxyl group, which induces a cyclization reaction on the N-terminal carbamate and releases a fluorescent reporter. Sequence selectivity is observed using several peptide substrates against alkaline phosphatase (ALP), bacteriophage lambda protein phosphatase (lambda-PPase), and vaccinia H1 related phosphatase (VHR). These studies suggest that the assay could be a useful tool for profiling the substrate specificities of medicinally important phosphatases.