N-(Trimethylsilyl)methionin-trimethylsilylester | 27844-10-6

• 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: N-(Trimethylsilyl)methionin-trimethylsilylester
• 英文别名: L-Methionine, N-(trimethylsilyl)-, trimethylsilyl ester；trimethylsilyl (2S)-4-methylsulfanyl-2-(trimethylsilylamino)butanoate
• CAS: 27844-10-6
• 化学式: C₁₁H₂₇NO₂SSi₂
• 分子量: 293.578
• InChiKey: JATQZWJTOMUJCG-JTQLQIEISA-N

物化性质

• 保留指数：
  1530;1516.78;1518.48;1527.51

计算性质

• 辛醇/水分配系数(LogP)：
  2.91
• 重原子数：
  17
• 可旋转键数：
  8
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.91
• 拓扑面积：
  63.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-(Trimethylsilyl)methionin-trimethylsilylester 在 吗啉 、 四(三苯基膦)钯 、 lipase from Mucor miehei 、 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 三乙胺 、 N,N'-二环己基碳二亚胺 、 potassium iodide 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 61.5h， 生成 N-[4-(acetoxy)benzyloxycarbonyl]-glycyl-(S-palmitoyl)-L-cysteyl-L-methionyl-glycyl-L-leucyl-L-prolyl-(S-farnesyl)-L-cysteine methyl ester
  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-蛋氨酸 以 四氢呋喃 为溶剂， 反应 0.5h， 生成 N-(Trimethylsilyl)methionin-trimethylsilylester
  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

文献信息

• Synthese von geschützten Asparagin-Glycopeptiden durch N-terminale Peptidketten- Verlängerung. _ Teilsequenzen der Rinder-Desoxyribonuclease A und des luteinisierenden Hormons
  作者：Horst Kunz、Hermann Kauth

  DOI：10.1002/jlac.198319830302

  日期：1983.3.15

  bleiben. Durch Kondensation von 22 mit Peoc-Aminosäuren 8 entstehen die voll geschützten N4-Glycosylasparagin-Dipetide 24 und 30. Bei Kondensation der N2 deblockierten N4-Glycosylasparaginester 22 mit den Peoc-Peptiden 13b oder 13c werden die geschützten Glycotripeptide 28 bzw. 31 gebildet, die Partialsequenzen aus der Rinder-Desoxyribonucloase A bzw. der LH-β-Untereinheit darstellen. Auch kann von dem

  用2-乙酰氨基-3,4,6-三-O-乙酰基-2处理N- [2-（三苯基膦酰基）乙氧羰基]-[Peoc-]天冬氨酸苄酯（8h）和叔丁酯（8i）。 -脱氧-β-D-吡喃葡萄糖胺（2）与N 4 -glycosylasparagine衍生物相连19。从这些中，可以用二乙胺/叔丁醇或吗啉/二氯甲烷选择性地分离Peoc基团，所有其他保护基团和糖苷键保留在形成的N 4-糖基鞘氨醇酯22中。完全保护的N 4由22与Peoc氨基酸8的缩合形成-糖基天冬酰胺二肽24和30。在N 2解封闭的N 4糖基葡聚糖天冬酰胺酯22与Peoc肽13b或13c缩合时，形成被保护的糖三肽28和31，其代表来自牛脱氧核糖核酸酶A和LH-β亚基的部分序列。也可以从Peoc糖基肽叔丁酯30a高度选择性地切除N端Peoc基团，其结果是可以将肽链进一步延长至31。
• Cephalosporin isocyanates
  申请人：American Home Products Corporation

  公开号：US03932391A1

  公开（公告）日：1976-01-13

  Novel penicillin and cephalosporin isocyanates are described which are useful intermediates for reaction with compounds containing an active hydrogen to produce penicillin and cephalosporin derivatives having activity against gram positive and/or gram negative bacteria.

  描述了一种新的青霉素和头孢菌素异氰酸酯，这些异氰酸酯是有用的中间体，可与含有活性氢的化合物反应，产生对革兰氏阳性和/或革兰氏阴性细菌具有活性的青霉素和头孢菌素衍生物。
• Kunz, Horst; Schaumloeffel, Guenter, Liebigs Annalen der Chemie, 1985, # 9, p. 1784 - 1793
  作者：Kunz, Horst、Schaumloeffel, Guenter

  DOI：——

  日期：——
• DAVIDOVICH YU. A.; PAVLOVA L. A.; VOLKONSKIJ A. YU.; ROGOZHIN S. V., XIMIYA GETEROTSIKL. SOEDIN., 1978, HO 11, 1472-1473
  作者：DAVIDOVICH YU. A.、 PAVLOVA L. A.、 VOLKONSKIJ A. YU.、 ROGOZHIN S. V.

  DOI：——

  日期：——
• 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.