Benzyloxycarbonyl L-phenylalanine 4-Methylcoumaryl-7-amide | 75957-51-6

• 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: Benzyloxycarbonyl L-phenylalanine 4-Methylcoumaryl-7-amide
• 英文别名: Cbz-Phe-4-methylcoumarin-7-amide；benzyl N-[(2S)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxo-3-phenylpropan-2-yl]carbamate
• CAS: 75957-51-6
• 化学式: C₂₇H₂₄N₂O₅
• 分子量: 456.498
• InChiKey: ZZYFWHJZWFSUJD-QHCPKHFHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  34
• 可旋转键数：
  8
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.15
• 拓扑面积：
  93.7
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  7-氨基-4-甲基香豆素 、 N-苄氧羰基-L-苯丙氨酸 在 Bacillus licheniformis serine protease Alcalase cross-linked enzyme aggregate 作用下， 以 甲基叔丁基醚 为溶剂， 反应 16.0h， 以51%的产率得到Benzyloxycarbonyl L-phenylalanine 4-Methylcoumaryl-7-amide
  参考文献：
  名称：

  Enzymatic Synthesis of C-Terminal Arylamides of Amino Acids and Peptides

  摘要：

  A mild and cost-efficient chemo-enzymatic method for the synthesis of C-terminal arylamides of amino acid and peptides is described. Using the industrial serine protease Alcalase under near-anhydrous conditions, C-terminal arylamides of N-Cbz-protected amino acids and peptides could be obtained from the corresponding C-terminal carboxylic acids, methyl (Me) or benzyl (Bn) esters, in hi-h chemical and enantio- and diastereomeric purities. Yields ranged between 50% and 95% depending on the size of the aryl substituents and the presence of electron-withdrawing substituents. Complete (alpha-C-terminal selectivity could be obtained even in the presence of various unprotected side-chain functionalities such as beta/gamma-carboxyl, hydroxyl, and guanidino groups. In addition, the use of the cysteine protease papain and the lipase Cal-B gave anilides in high yields. The chemo-enzymatic synthesis of arylamides proved to be completely free of racemization, in contrast to the state-of-the-art chemical methods.

  DOI：

  10.1021/jo900634g

文献信息

• A Convenient Synthesis of Benzyloxycarbonyl-L-amino Acid 4-Methylcoumaryl-7-amides
  作者：S. Khammungkhune、G. Sigler

  DOI：10.1055/s-1980-29136

  日期：——
• POZDNEV, V. F.
  作者：POZDNEV, V. F.

  DOI：——

  日期：——
• [EN] CHEMO-ENZYMATIC SYNTHESIS OF A C-TERMINAL ARYL AMIDE OF AN AMINO ACID OR PEPTIDE<br/>[FR] SYNTHÈSE CHIMIO-ENZYMATIQUE D'UN ARYLAMIDE DE C-TERMINAL D'UN ACIDE AMINÉ OU PEPTIDE
  申请人：DSM IP ASSETS BV

  公开号：WO2009080631A2

  公开（公告）日：2009-07-02

  The present invention relates to a method for preparing an aryl amide, comprising reacting an aryl amine with a compound selected from N-protected amino acids and optionally N-protected peptides in the presence of a hydrolytic enzyme. The invention further relates to the use of a compound obtained in a method according to the invention in the manufacture of a diagnostic. In addition the invention relates to the use of a compound obtained in a method according to the invention as a substrate for a proteolytic enzyme.
• Enzymatic Synthesis of <i>C</i>-Terminal Arylamides of Amino Acids and Peptides
  作者：Timo Nuijens、Claudia Cusan、John A. W. Kruijtzer、Dirk T. S. Rijkers、Rob M. J. Liskamp、Peter J. L. M. Quaedflieg

  DOI：10.1021/jo900634g

  日期：2009.8.7

  A mild and cost-efficient chemo-enzymatic method for the synthesis of C-terminal arylamides of amino acid and peptides is described. Using the industrial serine protease Alcalase under near-anhydrous conditions, C-terminal arylamides of N-Cbz-protected amino acids and peptides could be obtained from the corresponding C-terminal carboxylic acids, methyl (Me) or benzyl (Bn) esters, in hi-h chemical and enantio- and diastereomeric purities. Yields ranged between 50% and 95% depending on the size of the aryl substituents and the presence of electron-withdrawing substituents. Complete (alpha-C-terminal selectivity could be obtained even in the presence of various unprotected side-chain functionalities such as beta/gamma-carboxyl, hydroxyl, and guanidino groups. In addition, the use of the cysteine protease papain and the lipase Cal-B gave anilides in high yields. The chemo-enzymatic synthesis of arylamides proved to be completely free of racemization, in contrast to the state-of-the-art chemical methods.