Bz-L-Tyr-L-Phe-NH2 | 119153-83-2

• 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: Bz-L-Tyr-L-Phe-NH2
• 英文别名: Bz-Tyr-Phe-NH2；N-[(2S)-1-[[(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]benzamide
• CAS: 119153-83-2
• 化学式: C₂₅H₂₅N₃O₄
• 分子量: 431.491
• InChiKey: ZGYGYCMQIFYHCL-VXKWHMMOSA-N

物化性质

• 熔点：
  268-270 °C
• 沸点：
  838.9±65.0 °C(Predicted)
• 密度：
  1.270±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  32
• 可旋转键数：
  9
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.16
• 拓扑面积：
  122
• 氢给体数：
  4
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  L-苯丙氨酰胺 、 N-苯甲酰-L-酪氨酸乙酯 在 α-chymotrypsin chemically modified with monomethoxypolyethylene glycol (α-CT-PEG) 作用下， 以 三氯乙烷 、 水 为溶剂， 反应 20.0h， 以95%的产率得到Bz-L-Tyr-L-Phe-NH2
  参考文献：
  名称：

  化学修饰的α-胰凝乳蛋白酶的化学选择性

  摘要：

  讨论了用单甲氧基聚乙二醇（α-CT-PEG）化学修饰的α-胰凝乳蛋白酶的酶活性，该酶以不同于天然酶底物的酯水解和肽合成为测试反应。这些反应允许分析α-CT-PEG的“ ar”，“ h”，“ n”和“ am”亚位的尺寸。使用2-氨基乙醇酸酯和甘氨酸衍生物，我们已经证明，化学修饰的α-CT（α-CT-PEG）的“ n”亚位的深度必须小于14.455Å，因为未观察到肽的合成。 2-氨基乙醇辛酸酯作为亲核试剂。α-CT-PEG对芳族酯具有化学选择性，因为非天然脂族酯在N-苯甲酰基-L-酪氨酸乙酯存在下不会被水解。距离不自然的脂族酰基供体小于8.8的小分子被化学修饰的酶识别为酰基给体。从这些结果，我们可以得出结论，α-CT-PEG不必识别酰基供体分子中N-酰基的存在。酰基供体和亲核试剂中均存在庞大的烷基链，这会降低酯水解和肽合成过程中生物催化剂的酶促活性。

  DOI：

  10.1016/0040-4020(94)01060-d

文献信息

• Chemoselectivity of chemically modified α-chymotrypsin
  作者：A. Dominguez、N. Cabezas、J.M. Sánchez - Montero、J.V. Sinisterra

  DOI：10.1016/0040-4020(94)01060-d

  日期：1995.2

  modified α-CT (α-CT-PEG) must be lower than 14.455 Å because the synthesis of peptides is not observed using 2-aminoethanol octanoate as nucleophile. α-CT-PEG is chemoselective towards the aromatic esters because unnatural aliphatic esters are not hydrolyzed in the presence of N-benzoyl-L-Tyrosine ethyl ester. Unnatural aliphatic acyl-donors with a distance smaller than 8.8 Å are recognized by the chemically

  讨论了用单甲氧基聚乙二醇（α-CT-PEG）化学修饰的α-胰凝乳蛋白酶的酶活性，该酶以不同于天然酶底物的酯水解和肽合成为测试反应。这些反应允许分析α-CT-PEG的“ ar”，“ h”，“ n”和“ am”亚位的尺寸。使用2-氨基乙醇酸酯和甘氨酸衍生物，我们已经证明，化学修饰的α-CT（α-CT-PEG）的“ n”亚位的深度必须小于14.455Å，因为未观察到肽的合成。 2-氨基乙醇辛酸酯作为亲核试剂。α-CT-PEG对芳族酯具有化学选择性，因为非天然脂族酯在N-苯甲酰基-L-酪氨酸乙酯存在下不会被水解。距离不自然的脂族酰基供体小于8.8的小分子被化学修饰的酶识别为酰基给体。从这些结果，我们可以得出结论，α-CT-PEG不必识别酰基供体分子中N-酰基的存在。酰基供体和亲核试剂中均存在庞大的烷基链，这会降低酯水解和肽合成过程中生物催化剂的酶促活性。
• Peptide synthesis catalyzed by modified .alpha.-chymotrypsin in low-water organic media
  作者：H. Gaertner、T. Watanabe、J. V. Sinisterra、A. Puigserver

  DOI：10.1021/jo00009a041

  日期：1991.4

  Enzyme-catalyzed synthesis of peptide bonds in organic solvents has been investigated by using alpha-chymotrypsin either modified with poly(ethylene glycol) or immobilized on different supports, in order to find out the importance of water content in the reaction. High yields of peptide synthesis were obtained whatever the type of enzyme derivative used. By varying the type of support, a modification in the enzyme environment was observed and resulted in a significant increase in the reaction yield when nucleophiles with poor affinity for the enzyme were used. Since organic solvents also affected substrate specificity with respect to the donor ester, a general methodology was proposed for the enzymatic synthesis of peptides in low-water organic media.
• Paradkar, Vikram M.; Dordick, Jonathan S., Journal of the American Chemical Society, 1994, vol. 116, # 11, p. 5009 - 5010
  作者：Paradkar, Vikram M.、Dordick, Jonathan S.

  DOI：——

  日期：——
• RICCA, J. M.;CROUT, D. H. G., J. CHEM. SOC. PERKIN TRANS. PT 1,(1989) N1, C. 2126-2127
  作者：RICCA, J. M.、CROUT, D. H. G.

  DOI：——

  日期：——
• Highly concentrated water-in-oil emulsions as novel reaction media for protease-catalysed kinetically controlled peptide synthesis
  作者：Pere Clapés、Laia Espelt、M Antonia Navarro、Conxita Solans

  DOI：10.1039/b100784j

  日期：——

  High-internal-phase-ratio-emulsions (HIPREs) or gel emulsions, formulated with a large amount of water (80.0–99.5% w/w), were investigated as reaction media for α-chymotrypsin-catalysed peptide synthesis under kinetic control using Ac-L-Phe-OEt and H-L-Leu-NH2 as model substrates. Both the initial reaction rate and dipeptide yield were examined as a function of the structure of the non-ionic polyoxyethylene alkyl ether type surfactant, alkyl chain length of the oil component, temperature and aqueous buffer content. Dipeptide yields of 70% were achieved in gel emulsions formulated with 90% w/w aqueous buffer. In these systems, the reaction performance was found to be independent of the gel emulsion system (i.e. surfactant and oil) and therefore of the water–oil interfacial tension. Interestingly, α-chymotrypsin showed superactivity at surfactant concentrations ranging between 0.2 and 0.8% w/w, that is, at 99.5 and 98.0% w/w water content, respectively. Furthermore, high dipeptide yields (90–94%) were achieved in the gel emulsions studied at very high substrate concentrations and thus with undissolved reactants. Under these conditions, examples of α-chymotrypsin-catalysed dipeptide synthesis on an analytical and preparative scale were conducted.

  使用大量水（80.0–99.5% w/w）配制的高内相比乳液 (HIPRE) 或凝胶乳液作为反应介质，在动力学控制下研究了 α-胰凝乳蛋白酶催化的肽合成Ac-L-Phe-OEt 和 H-L-Leu-NH2 作为模型底物。检测初始反应速率和二肽产率作为非离子聚氧乙烯烷基醚型表面活性剂的结构、油组分的烷基链长度、温度和水性缓冲液含量的函数。在用 90% w/w 水性缓冲液配制的凝胶乳液中，二肽产率达到 70%。在这些系统中，发现反应性能与凝胶乳液系统（即表面活性剂和油）无关，因此与水油界面张力无关。有趣的是，α-胰凝乳蛋白酶在表面活性剂浓度范围为 0.2 至 0.8% w/w（即 99.5）时表现出超活性。 和 98.0% w/w 含水量。此外，在非常高的底物浓度和不溶解的反应物下研究的凝胶乳液中实现了高二肽产率（90-94%）。在这些条件下，进行了分析和制备规模的 α-胰凝乳蛋白酶催化二肽合成的实例。