trimethylsilyl (2S)-3-hydroxy-2-(trimethylsilylamino)propanoate | 70125-39-2

• 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: trimethylsilyl (2S)-3-hydroxy-2-(trimethylsilylamino)propanoate
• CAS: 70125-39-2
• 化学式: C₉H₂₃NO₃Si₂
• 分子量: 249.458
• InChiKey: PYMNNGBEFDDKPA-QMMMGPOBSA-N

物化性质

• 沸点：
  245.1±35.0 °C(Predicted)
• 密度：
  0.964±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.15
• 重原子数：
  15
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.89
• 拓扑面积：
  58.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  trimethylsilyl (2S)-3-hydroxy-2-(trimethylsilylamino)propanoate 、 4-(acetoxy)benzyl chloroformate 在 三乙胺 作用下， 以 四氢呋喃 为溶剂， 生成 (S)-2-(4-Acetoxy-benzyloxycarbonylamino)-3-hydroxy-propionic acid
  参考文献：
  名称：

  Chemoenzymatic Synthesis of N-Ras Lipopeptides

  摘要：

  For the study of biological phenomena influenced by the plasma-membrane-bound Ras proteins and other lipidated proteins, characteristic peptides which embody the correct lipid modifications of their parent proteins (palmitoyl thioesters and farnesyl thioethers), as well as analogues thereof, may serve as suitable tools. For the construction of such acid- and base-labile peptide conjugates, the enzyme-labile p-acetoxybenzyloxycarbonyl (AcOZ) urethane blocking group was developed. The acetate moiety within the AcOZ group is easily saponified by treatment with acetyl esterase or lipase. After cleavage of the acetate group the resulting quinone methide spontaneously fragments, resulting in the liberation of the desired peptide or peptide conjugates. This enzymatic protecting group technique formed the key step in the synthesis of the characteristic S-palmitoylated and S-farnesylated C-terminus of the human N-Ras protein. Deprotections are so mild that no undesired side reactions of the lipid conjugates are observed (i.e., no hydrolysis or beta-elimination of the thioester and no acid-mediated attack on the double bonds of the farnesyl group). The combination of enzymatic protecting group techniques with classical chemical methods allowed access to various fluorescent-labeled and differently lipid-modified Rns lipopeptides. Their application in biological experiments enabeled the study of the structural requirements for the acylation of Ras sequence motifs in vivo and gave insight into the subcellular site at which these modifications occur. The results indicate that the plasma membrane is a major site of cellular S-acylation. This supports a mechanism for the selective subcellular localization of lipidated proteins, including the Rns proteins themselves, by kinetic targeting to the plasma membrane.

  DOI：

  10.1021/ja9805627
• 作为产物：
  描述：

  三甲基氯硅烷 、 L-丝氨酸 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 1.0h， 生成 trimethylsilyl (2S)-3-hydroxy-2-(trimethylsilylamino)propanoate
  参考文献：
  名称：

  Suresh Babu, Vommina V.; Kantharaju, Indian Journal of Chemistry - Section B Organic and Medicinal Chemistry, 2005, vol. 44, # 5, p. 1046 - 1053

  摘要：

  DOI：

文献信息

• δ¹³ C analysis of amino acids in human hair using trimethylsilyl derivatives and gas chromatography/combustion/isotope ratio mass spectrometry
  作者：Yan An、Zeland Schwartz、Glen P. Jackson

  DOI：10.1002/rcm.6592

  日期：2013.7.15

  derivatization procedure for the analysis of a wide variety of amino acids in human hair by gas chromatography/combustion/isotope ratio mass spectrometry (GC/C/IRMS). N,O‐Bis(trimethylsilyl)trifluoroacetamide (BSTFA) derivatization is already widely used outside the IRMS community, is applicable to a variety of functional groups, and provides products that are common entries in mass spectral databases, thus

  通过气相色谱/燃烧/同位素比质谱（GC / C / IRMS），为分析人发中的多种氨基酸提供简单的一步衍生化程序。N，O-双（三甲基甲硅烷基）三氟乙酰胺（BSTFA）衍生化已在IRMS社区之外广泛使用，适用于各种官能团，并提供了质谱数据库中常见条目的产品，从而简化了化合物鉴定。
• Chemoenzymatic Synthesis of N-<i>Ras</i> Lipopeptides
  作者：Edgar Nägele、Michael Schelhaas、Norman Kuder、Herbert Waldmann

  DOI：10.1021/ja9805627

  日期：1998.7.1

  For the study of biological phenomena influenced by the plasma-membrane-bound Ras proteins and other lipidated proteins, characteristic peptides which embody the correct lipid modifications of their parent proteins (palmitoyl thioesters and farnesyl thioethers), as well as analogues thereof, may serve as suitable tools. For the construction of such acid- and base-labile peptide conjugates, the enzyme-labile p-acetoxybenzyloxycarbonyl (AcOZ) urethane blocking group was developed. The acetate moiety within the AcOZ group is easily saponified by treatment with acetyl esterase or lipase. After cleavage of the acetate group the resulting quinone methide spontaneously fragments, resulting in the liberation of the desired peptide or peptide conjugates. This enzymatic protecting group technique formed the key step in the synthesis of the characteristic S-palmitoylated and S-farnesylated C-terminus of the human N-Ras protein. Deprotections are so mild that no undesired side reactions of the lipid conjugates are observed (i.e., no hydrolysis or beta-elimination of the thioester and no acid-mediated attack on the double bonds of the farnesyl group). The combination of enzymatic protecting group techniques with classical chemical methods allowed access to various fluorescent-labeled and differently lipid-modified Rns lipopeptides. Their application in biological experiments enabeled the study of the structural requirements for the acylation of Ras sequence motifs in vivo and gave insight into the subcellular site at which these modifications occur. The results indicate that the plasma membrane is a major site of cellular S-acylation. This supports a mechanism for the selective subcellular localization of lipidated proteins, including the Rns proteins themselves, by kinetic targeting to the plasma membrane.
• Suresh Babu, Vommina V.; Kantharaju, Indian Journal of Chemistry - Section B Organic and Medicinal Chemistry, 2005, vol. 44, # 5, p. 1046 - 1053
  作者：Suresh Babu, Vommina V.、Kantharaju

  DOI：——

  日期：——