Cbz-Ser-Gly-O^tBu | 30735-47-8

• 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: Cbz-Ser-Gly-O^tBu
• 英文别名: tert-butyl 2-[[(2S)-3-hydroxy-2-(phenylmethoxycarbonylamino)propanoyl]amino]acetate
• CAS: 30735-47-8
• 化学式: C₁₇H₂₄N₂O₆
• 分子量: 352.387
• InChiKey: MSKQEWCLELYPRI-ZDUSSCGKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  25
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  114
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  Cbz-Ser-Gly-O^tBu 在 palladium on activated charcoal 三氟化硼乙醚 、 氢气 作用下， 以 甲醇 、 二氯甲烷 、 环己烷 为溶剂， 反应 17.0h， 生成 L-Seryl(O-tert-butyl)-glycine tert-butyl ester hydrotosylate
  参考文献：
  名称：

  Enzymatic Protecting Group Techniques for Glyco- and Phosphopeptide Chemistry: Synthesis of a Glycophosphopeptide from Human Serum Response Factor

  摘要：

  The covalent modification of proteins by phosphorylation and by glycosylation with GlcNAc residues are important regulatory processes which mediate biological signal transduction. For the study of such biological phenomena in molecular detail characteristic peptides which embody both types of modification may serve as efficient tools. However, their synthesis is complicated by their pronounced acid and base lability as well as their multifunctionality. For this purpose the enzyme labile choline ester was developed. The choline ester can be removed selectively and in high yields from various GlcNAc-glycopeptides and phosphopeptides at pH 6.5 and 37 degrees C. The conditions under which the enzymatic deprotections proceed are so mild that no undesirable side reactions are observed (i.e., no cleavage or anomerization of the glycosidic bonds and no beta-elimination of the phosphate or the carbohydrate occur). The specificity of the biocatalyst guarantees that neither the peptide bonds nor the other protecting groups present are being attacked. When this enzymatic protecting group technique was combined with the enzyme-labile 4-(phenylacetoxy)benzyloxycarbonyl (PhAcOZ) urethane protecting group a complex glycophosphopeptide could be built up. The glycopeptide is equipped with a biotin label by which it can be traced in biological systems. This peptide represents a characteristic partial structure of a glycosylated and phosphorylated sequence from the transactivation domain of serum response factor (SRF), a widely occuring human transcription factor.

  DOI：

  10.1002/(sici)1521-3765(20000502)6:9<1564::aid-chem1564>3.3.co;2-h
• 作为产物：
  描述：

  甘氨酸叔丁酯盐酸盐 在 2-溴-4-(三氟甲基)苯硼酸 、 sodium carbonate 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 24.08h， 生成 Cbz-Ser-Gly-O^tBu
  参考文献：
  名称：

  通过硼酸催化从α-氨基酸衍生的惰性酯形成羟基引导的肽键

  摘要：

  描述了硼酸催化 α-氨基酸甲酯形成肽键。该催化对 β-羟基-α-氨基酯表现出高化学选择性，使肽具有高至优异的产率和高官能团耐受性。这种羟基定向的肽键形成可适用于寡肽合成。这是有机硼催化α-氨基酸衍生的惰性酯形成肽键的第一个成功例子。

  DOI：

  10.1039/d3cc04856j

文献信息

• Acyl transfer from carboxylate, carbonate, and thiocarbonate esters to enzymatic and nonenzymatic thiolates
  作者：Christian Gravel、Danielle Lapierre、Judith Labelle、Jeffrey W Keillor

  DOI：10.1139/v07-011

  日期：2007.3.1

  pep- tide-bound glutamine residues as acyl donors and peptide-bound lysine residues as acyl acceptors, resulting in the for- mation of intermolecular e-(γ-glutamyl)lysine crosslinks. The mechanistic details of its "ping-pong" transamidation reaction remain unknown. In particular, few studies have been published probing the nucleophilicity of TGase using acyl-donor substrates of varied electrophilicity

  转谷氨酰胺酶 (EC 2.3.2.13) (TGases) 催化作为酰基供体的肽结合谷氨酰胺残基和作为酰基受体的肽结合赖氨酸残基之间的钙依赖性酰基转移反应，导致分子间 e-(γ -谷氨酰）赖氨酸交联。其“乒乓”转酰胺反应的机制细节仍然未知。特别是，很少有研究使用不同亲电性的酰基供体底物来探索 TGase 的亲核性。在此，我们报告了碳酸酯、氨基甲酸酯和硫代碳酸酯的活化酯的合成及其与简单硫醇的反应，作为非酶参考点，以及与豚鼠肝脏 TGase 的催化半胱氨酸残基的反应。我们的动力学结果表明，侧链亚甲基单元被氧或硫的简单取代对底物亲和力和酰化反应性具有惊人的影响。此外，它们提供了对侧链杂原子赋予组织 TGase 亲和力的重要性的意外见解，并揭示了一类有趣的不可逆抑制剂。
• Diboronic Acid Anhydride-Catalyzed Direct Peptide Bond Formation Enabled by Hydroxy-Directed Dehydrative Condensation
  作者：Masayoshi Koshizuka、Kazuishi Makino、Naoyuki Shimada

  DOI：10.1021/acs.orglett.0c03252

  日期：2020.11.6

  We report the catalytic direct peptide bond formations via dehydrative condensation of β-hydroxy-α-amino acids, affording the serine, threonine, or β-hydroxyvaline-derived peptides in high to excellent yields with high functional group tolerance, minimum epimerization, and excellent chemoselectivity. The key to the success of these atom-economical transformations is the use of diboronic acid anhydride catalyst for the hydroxy-directed reactions.
• Enzymatic Protecting Group Techniques for Glyco- and Phosphopeptide Chemistry: Synthesis of a Glycophosphopeptide from Human Serum Response Factor
  作者：Jörg Sander、Herbert Waldmann

  DOI：10.1002/(sici)1521-3765(20000502)6:9<1564::aid-chem1564>3.3.co;2-h

  日期：2000.5.2

  The covalent modification of proteins by phosphorylation and by glycosylation with GlcNAc residues are important regulatory processes which mediate biological signal transduction. For the study of such biological phenomena in molecular detail characteristic peptides which embody both types of modification may serve as efficient tools. However, their synthesis is complicated by their pronounced acid and base lability as well as their multifunctionality. For this purpose the enzyme labile choline ester was developed. The choline ester can be removed selectively and in high yields from various GlcNAc-glycopeptides and phosphopeptides at pH 6.5 and 37 degrees C. The conditions under which the enzymatic deprotections proceed are so mild that no undesirable side reactions are observed (i.e., no cleavage or anomerization of the glycosidic bonds and no beta-elimination of the phosphate or the carbohydrate occur). The specificity of the biocatalyst guarantees that neither the peptide bonds nor the other protecting groups present are being attacked. When this enzymatic protecting group technique was combined with the enzyme-labile 4-(phenylacetoxy)benzyloxycarbonyl (PhAcOZ) urethane protecting group a complex glycophosphopeptide could be built up. The glycopeptide is equipped with a biotin label by which it can be traced in biological systems. This peptide represents a characteristic partial structure of a glycosylated and phosphorylated sequence from the transactivation domain of serum response factor (SRF), a widely occuring human transcription factor.
• Hydroxy-directed peptide bond formation from α-amino acid-derived inert esters enabled by boronic acid catalysis
  作者：Naoya Takahashi、Airi Takahashi、Naoyuki Shimada

  DOI：10.1039/d3cc04856j

  日期：——

  acid-catalyzed peptide bond formation from α-amino acid methyl esters is described. The catalysis showed high chemoselectivity for β-hydroxy-α-amino esters, affording the peptides in high to excellent yields with high functional group tolerance. This hydroxy-directed peptide bond formation could be applicable to oligopeptide syntheses. This is the first successful example of organoboron-catalyzed peptide bond

  描述了硼酸催化 α-氨基酸甲酯形成肽键。该催化对 β-羟基-α-氨基酯表现出高化学选择性，使肽具有高至优异的产率和高官能团耐受性。这种羟基定向的肽键形成可适用于寡肽合成。这是有机硼催化α-氨基酸衍生的惰性酯形成肽键的第一个成功例子。