2-bromoethyl (2S,3S)-2-amino-3-methylpentanoate | 71283-17-5

• 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: 2-bromoethyl (2S,3S)-2-amino-3-methylpentanoate
• CAS: 71283-17-5
• 化学式: C₈H₁₆BrNO₂
• 分子量: 238.125
• InChiKey: ZOACKMIQPJTDAN-BQBZGAKWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  12
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  52.3
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-bromoethyl (2S,3S)-2-amino-3-methylpentanoate 在 氢溴酸 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二异丙基碳二亚胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 水 、 溶剂黄146 、 N,N-二甲基甲酰胺 、 丙酮 为溶剂， 反应 121.0h， 生成 N-Benzyloxycarbonyl-L-seryl(O-2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-L-isoleucine choline ester bromide
  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：

  L-异亮氨酸 、 2-溴乙醇 在 氯化亚砜 作用下， 生成 2-bromoethyl (2S,3S)-2-amino-3-methylpentanoate
  参考文献：
  名称：

  Kunz,H.; Buchholz,M., Chemische Berichte, 1979, vol. 112, p. 2145 - 2157

  摘要：

  DOI：

文献信息

• Kunz,H.; Buchholz,M., Chemische Berichte, 1979, vol. 112, p. 2145 - 2157
  作者：Kunz,H.、Buchholz,M.

  DOI：——

  日期：——
• 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.