Z-Phe-Leu-OBzl | 60641-89-6

• 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: Z-Phe-Leu-OBzl
• 英文别名: N-(benzyloxycarbonyl)phenylalanylleucine benzyl ester；Cbz-Phe-Leu-OBn；benzyl (2S)-4-methyl-2-[[(2S)-3-phenyl-2-(phenylmethoxycarbonylamino)propanoyl]amino]pentanoate
• CAS: 60641-89-6
• 化学式: C₃₀H₃₄N₂O₅
• 分子量: 502.61
• InChiKey: WMOZCMSOFNBHTJ-SVBPBHIXSA-N

物化性质

• 沸点：
  693.0±55.0 °C(Predicted)
• 密度：
  1.164±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.9
• 重原子数：
  37
• 可旋转键数：
  14
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  93.7
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  Z-Phe-Leu-OBzl 在 phosphate buffer 、 Bacillus subtilis esterase 作用下， 以 甲醇 、 正己烷 为溶剂， 反应 24.0h， 以84%的产率得到N-[N-[(phenylmethoxy)carbonyl]-L-phenylalanyl]-L-leucine
  参考文献：
  名称：

  酶去除羧基保护基。2.裂解苄基和甲基部分

  摘要：

  酶是用于有效去除甲基和苄基保护基团的通用试剂。来自枯草芽孢杆菌的酯酶（BS2）和来自南极假丝酵母的脂肪酶（CAL-A）可以高产率温和而选择性地除去这些部分，而不会影响其他官能团。

  DOI：

  10.1021/jo051004v
• 作为产物：
  描述：

  N-苄氧羰基-L-苯丙氨酸 、 L-亮氨酸苄酯对甲苯磺酸盐 在 N-羟基-7-氮杂苯并三氮唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 为溶剂， 以100%的产率得到Z-Phe-Leu-OBzl
  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

• Fully Enzymatic Peptide Synthesis using C-Terminal tert-Butyl Ester Interconversion
  作者：Timo Nuijens、Claudia Cusan、Theodorus J. G. M. van Dooren、Harold M. Moody、Remco Merkx、John A. W. Kruijtzer、Dirk T. S. Rijkers、Rob M. J. Liskamp、Peter J. L. M. Quaedflieg

  DOI：10.1002/adsc.201000313

  日期：2010.10.4

  Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides with some important advantages. For instance, stoichiometric amounts of expensive coupling reagents are not required and racemisation does not occur, thus rendering purification easier compared to chemical peptide synthesis. The economically most attractive synthesis runs in the

  化学酶促肽合成可能是合成短和中等大小肽的最经济有效的技术，具有一些重要的优势。例如，不需要化学计量的昂贵偶联剂，也不会发生外消旋化，因此与化学肽合成相比，纯化更加容易。经济上最具吸引力的合成是在NC末端方向进行的，其中廉价的C末端保护的氨基酸被用作延伸的基础。然而，延长步骤后的C末端脱保护和激活-不会裂解侧链保护基或肽键-仍然是一个挑战。在本文中，我们描述了一种新颖的C丝氨酸内肽酶Alcalase催化末端酯的相互转化。C-末端保护的肽叔丁酯以定量收率被酶促转化为伯烷基酯，并与另一种氨基酸叔丁酯直接用于下一步的酶促延伸步骤。通过C-末端酯互变的这种完全酶促NC延伸策略被用于合成高达五聚体水平的生物活性肽。
• Versatile Selective α-Carboxylic Acid Esterification of N-Protected Amino Acids and Peptides by Alcalase
  作者：Peter Quaedflieg、Timo Nuijens、Claudia Cusan、John Kruijtzer、Dirk Rijkers、Rob Liskamp

  DOI：10.1055/s-0028-1083362

  日期：——

  water, the industrial protease Alcalase allows selective synthesis of α-carboxylic acid methyl, ethyl, benzyl, allyl, 2-(trimethylsilyl)ethyl, and tert-butyl esters of amino acids and peptides under mild conditions in very high yields. The purified yields range from 72% to 92%. enzymes - amino acids - esterification - esters - protecting groups

  在连续去除水的条件下，工业蛋白酶Alcalase可以在温和条件下以很高的收率选择性合成氨基酸和肽的α-羧酸甲酯，乙酯，苄酯，烯丙基，2-（三甲基甲硅烷基）乙酯和叔丁酯。纯化的产率为72％至92％。 酶-氨基酸-酯化-酯-保护基
• Conformational mimicry. 3. Synthesis and incorporation of 1,5-disubstituted tetrazole dipeptide analogs into peptides with preservation of chiral integrity: bradykinin
  作者：Janusz Zabrocki、James B. Dunbar、Keith W. Marshall、Mihaly V. Toth、Garland R. Marshall

  DOI：10.1021/jo00027a038

  日期：1992.1

  New synthetic procedures for preparing 1,5-disubstituted tetrazole dipeptide analogues, which are a conformational mimic of the cis amide bond, and incorporating these analogues into longer peptides, such as bradykinin, while maintaining chiral integrity are presented. The simple addition of the organic base, quinoline, to the reaction with PCl5 when generating an imidoyl chloride from the amide was effective in reducing racemization of the N-terminal amino acid residue of the protected tetrazole dipeptide to minimal levels. The resulting tetrazole dipeptide is quite sensitive to base, and the normal procedures of solid-phase synthesis for neutralization were sufficient to cause racemization of the alpha carbon on the C-terminal side of the tetrazole ring. The use of Z for amino protection and benzyl ester for carboxyl protection with differential removal of the Z group by HBr/HOAc has proven a practical route to a wide variety of tetrazole dipeptides. Immediate acylation of the tetrazole dipeptide with a Boc amino acid was necessary to prevent formation of the diketopiperazine, which is favored because of the cis conformation of the amide bond surrogate. Three bradykinin analogues, [L-Pro2-psi[CN4]-L-Ala3]-BK, [L-Ala6-psi[CN4]-L-Ala7]-BK, and [L-Ala6-psi[CN4]-D-Ala7]-BK, in which the peptide bond of a proline residue was replaced with the tetrazole surrogate, were prepared to illustrate the synthetic procedures. The availability of these procedures should increase the use of the tetrazole dipeptide analogue in molecular recognition studies.