N-Allyloxycarbonyl-L-threonine methyl ester | 221351-00-4

• 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-Allyloxycarbonyl-L-threonine methyl ester
• 英文别名: Alloc-L-Thr-OMe；Aloc-Thr-OMe；methyl (2S,3R)-3-hydroxy-2-(prop-2-enoxycarbonylamino)butanoate
• CAS: 221351-00-4
• 化学式: C₉H₁₅NO₅
• 分子量: 217.222
• InChiKey: HLRBFCCERJMPAL-RQJHMYQMSA-N

物化性质

• 沸点：
  359.6±42.0 °C(Predicted)
• 密度：
  1.166±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.3
• 重原子数：
  15
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  84.9
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-Allyloxycarbonyl-L-threonine methyl ester 在 四氮唑 、 L-半胱氨酸 、 butyrylcholine esterase 、 1-羟基苯并三唑 、 三乙胺 、 间氯过氧苯甲酸 、 papain 、 N,N'-二异丙基碳二亚胺 作用下， 以 phosphate buffer 、 二氯甲烷 、 丙酮 为溶剂， 反应 144.0h， 生成 N-Allyloxycarbonyl-L-threonyl(O-diallylphosphato)-L-glutaminyl-L-threonine
  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-苏氨酸甲酯 、 氯甲酸烯丙酯 在 三乙胺 作用下， 以 乙腈 为溶剂， 反应 18.5h， 以98%的产率得到N-Allyloxycarbonyl-L-threonine methyl ester
  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

文献信息

• Convergent Synthesis of Calcium-Dependent Antibiotic CDA3a and Analogues with Improved Antibacterial Activity via Late-Stage Serine Ligation
  作者：Delin Chen、Kathy Hiu Laam Po、Pilar Blasco、Sheng Chen、Xuechen Li

  DOI：10.1021/acs.orglett.0c01544

  日期：2020.6.19

  A convergent synthesis via the late-stage serine ligation of naturally occurring calcium-dependent antibiotic CDA3a and its analogues has been developed, which allowed us to readily synthesize the analogues with the variation on the lipid tail. Some analogues were found to show 100–500-fold higher antimicrobial activity than the natural compound CDA3a against drug resistant bacteria. This study will

  已经开发了通过后期丝氨酸连接天然存在的钙依赖性抗生素CDA3a及其类似物的聚合合成方法，这使我们能够容易地合成具有脂质尾巴变异的类似物。发现某些类似物对天然抗药性细菌的抗菌活性比天然化合物CDA3a高100-500倍。这项研究将增进我们对CDA3a的了解，并为进一步开发提供有价值的抗菌先导候选物。
• Chemoenzymatic Synthesis of Nucleopeptides
  作者：Stefanie Flohr、Volker Jungmann、Herbert Waldmann

  DOI：10.1002/(sici)1521-3765(19990201)5:2<669::aid-chem669>3.0.co;2-v

  日期：1999.2.1

  Nucleoproteins, in which the hydroxy group of a serine, a threonine, or a tyrosine, is linked through a phosphodiester group to the 3'- or 5'-end of DNA or RNA, play decisive roles in important biological processes. They may even have a major part in the process of viral replication by nucleoprotein-primed elongation of the oligonucleotide strand. For the study of the biological phenomena, in which nucleoproteins are involved, nucleopeptides with the characteristic linkage between the peptide chain and the oligonucleotide of their parent nucleoproteins may serve as powerful tools. However, the synthesis of these compounds is complicated by their pronounced acid- and base-lability, as well as their multifunctionality. As a result, protecting groups, which can be removed under the mildest conditions, are required. For the construction of such peptide conjugates using a flexible building block strategy, a combination of enzyme-labile and chemical protecting groups was developed. The C-terminal blocking function can be removed selectively from fully protected nucleoamino acid methyl, 2-methoxyethyl (ME), and methoxyethoxyethyl (MEE) esters by saponification of the esters. After elongation of the peptide chain with amino acid or peptide methyl, ME, MEE, and choline esters, the C-terminal ester blocking group can again be removed easily. The methyl, ME, and MEE esters are cleaved off with lipase, and the choline ester group is selectively attacked by butyrylcholine esterase. The nucleoamino acids and peptides formed may be fully deprotected. To this end, the enzyme-labile N-phenylacetyl (PhAc) group, which was employed to mask the amino functions of the nucleobases, was removed. The O-acetate in the deoxyribose was saponified, and the allyl protecting groups present were cleaved by Pd-0-mediated allyl transfer. By combination of these techniques, a nucleopeptide was produced, which represents the characteristic linkage region of the nucleoprotein of adenovions 2. The conditions, under which the enzymatic deprotections proceed, are so mild that no undesired side reaction is observed, that is no depurination or beta elimination of the nucleosides occurs. In addition, the specificity of the biocatalysts ensures that the peptide bonds and the other protecting groups present are not attacked either.