Cbz-Leu-Phe-NH2 | 13171-96-5

• 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: Cbz-Leu-Phe-NH2
• 英文别名: Z-L-Leu-L-Phe-NH₂；N-(N-benzyloxycarbonyl-L-leucyl)-L-phenylalanine amide；N-(N-Benzyloxycarbonyl-L-leucyl)-L-phenylalanin-amid；Z-Leu-phe-NH2；benzyl N-[(2S)-1-[[(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate
• CAS: 13171-96-5
• 化学式: C₂₃H₂₉N₃O₄
• 分子量: 411.501
• InChiKey: IYWAYHYSFZQCSH-PMACEKPBSA-N

物化性质

• 沸点：
  686.4±55.0 °C(Predicted)
• 密度：
  1.170±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  30
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  111
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Cbz-Leu-Phe-NH2 在 papain potassium chloride 、 水 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以98%的产率得到苄氧羰基-亮氨酰-苯丙氨酸
  参考文献：
  名称：

  Zaher, M. R.; El-Sharief, A. M. Sh., Indian Journal of Chemistry - Section B Organic and Medicinal Chemistry, 1982, vol. 21, # 8, p. 740 - 743

  摘要：

  DOI：
• 作为产物：
  描述：

  苄氧羰基-亮氨酰-苯丙氨酸 在 orange flavedo peptide amidase 、 碳酸氢铵 作用下， 以 水 、 乙腈 为溶剂， 反应 72.0h， 以23%的产率得到Cbz-Leu-Phe-NH2
  参考文献：
  名称：

  C-Terminal Peptide Amidation Catalyzed by Orange Flavedo Peptide Amidase

  摘要：

  DOI：

  10.1002/(sici)1521-3773(19980803)37:13/14<1885::aid-anie1885>3.0.co;2-c

文献信息

• Efficient chemo-enzymatic synthesis of endomorphin-1 using organic solvent stable proteases to green the synthesis of the peptide
  作者：Honglin Sun、Bingfang He、Jiaxing Xu、Bin Wu、Pingkai Ouyang

  DOI：10.1039/c1gc15042a

  日期：——

  (Tyr-Pro-Trp-Phe-NH2, EM-1), an effective analgesic, was efficiently synthesized by a combination of enzymatic and chemical methods. Peptide Boc-Trp-Phe-NH2 was synthesized with a high yield of 97.1% by the solvent-stable protease WQ9-2 in a 20% methanol medium. The maximum concentration (141 g L−1) of Boc-Trp-Phe-NH2 was obtained with an economical molar ratio of the substrate of 1:1. The products crystallized

  内啡肽1（Tyr-Pro-Trp-Phe-NH 2，EM-1），有效 止痛药通过酶促方法和化学方法的有效合成。 肽类Boc-Trp-Phe-NH 2的合成产率高达97.1％。溶剂在20％甲醇培养基中的稳定蛋白酶WQ9-2。在经济的底物摩尔比为1 ：1的情况下，获得Boc-Trp-Phe-NH 2的最大浓度（141 g L -1）。纯化，然后通过以下方式删除Boc小组： 三氟乙酸 产生 色氨酸-苯丙氨酸-NH 2。使用高效混合碳酸酐 方法， Boc-Tyr-Pro-OH是化学合成的。通过另一种有机化合物合成了四肽Boc-Tyr-Pro-Trp-Phe-NH 2，收率为84.5％。溶剂耐蛋白酶，PT121，来自 Boc-Tyr-Pro-OH和Trp-Phe-NH 2在有机-水双相系统中，并用乙酸乙酯，移动合成的平衡。EM-1是通过从Boc-Tyr-Pro-Trp-Phe-NH 2中除去Boc基
• One-Step<i>C</i>-Terminal Deprotection and Activation of Peptides with Peptide Amidase from<i>Stenotrophomonas maltophilia</i>in Neat Organic Solvent
  作者：Muhammad I. Arif、Ana Toplak、Wiktor Szymanski、Ben L. Feringa、Timo Nuijens、Peter J. L. M. Quaedflieg、Bian Wu、Dick B. Janssen

  DOI：10.1002/adsc.201400109

  日期：2014.7.7

  found that this conversion is efficiently catalysed by Stenotrophomonas maltophilia peptide amidase in neat organic media. The system excludes the possibility of internal peptide cleavage as the enzyme lacks intrinsic protease activity. The produced peptide methyl ester was used for peptide chain extension in a kinetically controlled reaction by a thermostable protease.

  化学酶促肽合成是用于大规模低成本生产肽的快速发展的技术。作为传统C → N策略的替代方法，该策略在每个步骤中都使用昂贵的N保护基块，我们研究了一种N →C扩展途径，该途径基于将肽C-末端酰胺保护基激活为相应的甲基酯。我们发现，这种转化被嗜麦芽窄食单胞菌有效地催化了。纯有机介质中的肽酰胺酶。该系统排除了内部肽裂解的可能性，因为该酶缺乏固有的蛋白酶活性。产生的肽甲酯用于通过热稳定蛋白酶进行动力学控制的反应中的肽链延伸。
• Mechanoenzymatic peptide and amide bond formation
  作者：José G. Hernández、Karen J. Ardila-Fierro、Deborah Crawford、Stuart L. James、Carsten Bolm

  DOI：10.1039/c7gc00615b

  日期：——

  Mechanochemical chemoenzymatic peptide and amide bond formation catalysed by papain was studied by ball milling. Despite the high-energy mixing experienced inside the ball mill, the biocatalyst proved stable and highly efficient to catalyse the formation of α,α- and α,β-dipeptides. This strategy was further extended to the enzymatic acylation of amines by milling, and to the mechanosynthesis of a derivative

  通过球磨研究了木瓜蛋白酶催化的机械化学化学酶促肽和酰胺键的形成。尽管在球磨机内部经历了高能混合，但是生物催化剂被证明是稳定且高效的，以催化α，α-和α，β-二肽的形成。该策略进一步扩展到通过研磨将胺酶促酰化，并扩展到有价值的二肽L-丙氨酰基-L-谷氨酰胺衍生物的机械合成。
• Enzymatic C-terminal amidation of amino acids and peptides
  作者：Timo Nuijens、Elena Piva、John A.W. Kruijtzer、Dirk T.S. Rijkers、Rob M.J. Liskamp、Peter J.L.M. Quaedflieg

  DOI：10.1016/j.tetlet.2012.05.039

  日期：2012.7

  enzymatic approaches for the conversion of semi-protected amino acid and peptidyl C-terminal α-carboxylic acids into their corresponding amides. In the first approach, the lipase Candida antarctica lipase-B (Cal-B), and in the second approach, the protease Subtilisin A, are used, respectively. We found that by using the ammonium salt of the α-carboxylic acid instead of separate ammonia sources, the enzymatic

  在本文中，我们描述了两种通用且高产的酶促方法，可将半保护的氨基酸和肽基C末端α-羧酸转化为它们相应的酰胺。在第一种方法中，分别使用脂肪酶南极假丝酵母脂肪酶-B（Cal-B），在第二种方法中，分别使用蛋白酶枯草杆菌蛋白酶A。我们发现，通过使用α-羧酸的铵盐代替单独的氨源，酶促酰胺化反应的进行速度大大加快，而没有副反应，并且使产物收率接近定量。
• α-Chymotrypsin-catalyzed peptide synthesis in frozen aqueous solution using N-protected amino acid carbamoylmethyl esters as acyl donors
  作者：Sayed Mohiuddin Abdus Salam、Ken-ichi Kagawa、Katsuhiro Kawashiro

  DOI：10.1016/j.tetasy.2005.10.042

  日期：2006.1

  A kinetically controlled peptide synthesis catalyzed by alpha-chymotrypsin was performed in frozen aqueous solution (ice, -24 degrees C). The yield of the peptide was significantly improved by the use of the carbamoylmethyl (Cam) ester as the acyl donor instead of the conventional ethyl ester. The peptide yield increased up to ca. 90% when N-benzyloxycarbonyl (CBZ)-Phe-OCam and H-Phe-NH2 were used as the acyl donor and nucleophile, respectively. Such an improvement of the peptide yield in ice was also observed in the coupling of other CBZ-amino acid Cam esters as acyl donors. Furthermore, this approach was applied to the synthesis of peptides containing D-amino acids. The peptides such as CBZ-D-Phe-Phe-NH2, CBZ-Phe-D-Phe-NH2 and CBZ-D-Phe-D-Phe-NH2 were also obtained in excellent to moderate yields in ice. A high diastereoselectivity towards the L-L peptide was observed when the racemic amino acid Cam ester was used as the acyl donor in ice. (c) 2005 Elsevier Ltd. All rights reserved.