Z-Tyr-Gly-Gly-OEt | 34695-67-5

• 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: Z-Tyr-Gly-Gly-OEt
• 英文别名: ZTyrGlyGlyOEt；N-benzyloxycarbonyl-tyrosyl=>glycyl=>glycine ethyl ester；N-Benzyloxycarbonyl-tyrosyl=>glycyl=>glycin-aethylester；N-[N-(N-Benzyloxycarbonyl-L-tyrosyl)-glycyl]-glycin-aethylester；ethyl 2-[[2-[[(2S)-3-(4-hydroxyphenyl)-2-(phenylmethoxycarbonylamino)propanoyl]amino]acetyl]amino]acetate
• CAS: 34695-67-5
• 化学式: C₂₃H₂₇N₃O₇
• 分子量: 457.483
• InChiKey: JSGBSUOKSSRQMC-IBGZPJMESA-N

物化性质

• 熔点：
  165 °C
• 沸点：
  773.8±60.0 °C(Predicted)
• 密度：
  1.277±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  33
• 可旋转键数：
  13
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  143
• 氢给体数：
  4
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Z-Tyr-Gly-Gly-OEt 在 sodium hydroxide 、 四丁基氢氧化铵 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 N-benzyloxycarbonyl-L-tyrosyl-glycyl-glycyl-L-phenylalanyl-L-leucine benzyl ester
  参考文献：
  名称：

  使用苯基膦酸酯作为偶联剂合成肽

  摘要：

  通过在双（邻或对硝基苯基）苯基膦酸酯存在下用氨基酸酯处理 N-保护的氨基酸（或肽）的四丁基铵盐，可以有效地合成含有各种功能的肽。上述方法采用（3+2）或（4+1）片段偶联方法成功合成亮氨酸-脑啡肽。

  DOI：

  10.1246/cl.1981.65
• 作为产物：
  描述：

  N-[(苯基甲氧基)羰基]-L-酪氨酸乙酯 在 盐酸 、 乙醇 、 一水合肼 、 乙酸乙酯 、 sodium nitrite 作用下， 生成 Z-Tyr-Gly-Gly-OEt
  参考文献：
  名称：

  Bergmann; Fruton, Journal of Biological Chemistry, 1937, vol. 118, p. 405,414

  摘要：

  DOI：

文献信息

• Enzymatic syntheses of N-protected Leu-enkephalin and some oligopeptides in organic solvents
  作者：Yun-Hua Ye、Gui-Ling Tian、Guo-Wen Xing、Dong-Cheng Dai、Gang Chen、Chong-Xi Li

  DOI：10.1016/s0040-4020(98)00737-6

  日期：1998.10

  Enzymatic syntheses of bioacitive pentapeptide, N-protected Leu-enkephalin and some other oligopeptides in organic solvents were studied. The stereoselectivity of the enzymatic reaction was examined by using racemic substrates. Different enzymes, solvent systems and protecting groups were compared. The importance of the essential water was addressed. The side chain of tyrosine was not protected during

  研究了生物活性五肽，N-保护的亮脑啡肽和其他一些寡肽在有机溶剂中的酶促合成。通过使用外消旋底物检查酶促反应的立体选择性。比较了不同的酶，溶剂系统和保护基。讨论了必需水的重要性。在所有酶促反应过程中，酪氨酸的侧链均未得到保护。在混合溶剂或有机溶剂中，通过木瓜蛋白酶和α-胰凝乳蛋白酶将P-DL-AlaOY（P = Z或Boc，YH或Me）和P-DL-TyrOEt与GlyNHNHPh偶联，以获得所需的光学纯产物PL-AlaGlyNHNHPh和PL-TyrGlyNHNHPh分别以良好的收率。两个甜味剂前体，ZAspXaaOR（XaaOR = PheOMe或AlaOcHex）通过嗜热菌中合成叔对戊醇和一些反应条件进行了优化以获得最佳收率。使用α-胰凝乳蛋白酶和嗜热菌蛋白酶作为催化剂，在二氯甲烷和叔戊醇中，研究了N-保护的亮脑啡肽ZTyrGlyGlyPheLeuOH的完全酶促合成。
• Synthesis of a Precursor of Bioactive Pentapeptide OGP-(10-14) and the Fragment of Enkephalin Catalyzed by MCM-22 Immobilized or Free Proteases in Organic Solvents
  作者：Ping Liu、Yun-hua Ye、Gui-ling Tian、Kin-Sing Lee、Man-Sau Wong、Wai-hung Lo

  DOI：10.1055/s-2002-25762

  日期：——

  Full enzymatic synthesis of a precursor of osteogenic growth peptide fragment (10-14), Z-Tyr-Gly-Phe-Gly-Gly--OEt, was accomplished using immobilized proteases on molecular sieve MCM-22 by adsorption as catalyst via 3+2 synthetic route for the first time. The reuse time of immobilized enzyme was dependent on concrete reaction system. Compared with free enzyme, the reaction rate catalyzed by immobilized

  成骨生长肽片段 (10-14) 的前体 Z-Tyr-Gly-Phe-Gly-Gly--OEt 的全酶合成是使用固定化蛋白酶在分子筛 MCM-22 上通过吸附作为催化剂通过 3+ 2合成路线首次。固定化酶的重复使用时间取决于具体的反应体系。与游离酶相比，大多数情况下固定化酶催化的反应速率明显提高，合成产率也有所提高。含水量和Et 3 N的添加量对固定化酶合成OGP-(I 0-14)和脑啡肽等生物活性肽片段的影响与游离酶不同。
• Enzymatic Peptide Synthesis in Organic Solvent with Different Zeolites as Immobilization Matrixes
  作者：Guo-Wen Xing、Xuan-Wen Li、Gui-Ling Tian、Yun-Hua Ye

  DOI：10.1016/s0040-4020(00)00261-1

  日期：2000.5

  A series of zeolite immobilized α-chymotrypsin and thermolysin with microporous Y zeolites (HY, NH4Y, NaY) and mesoporous dealuminized DAY zeolites (HDAY, HNH4DAY) as matrixes have been prepared to catalyze peptide bond formation in organic solvents for the first time. The results indicated that most zeolite immobilized enzymes were active for peptide syntheses in organic media, and still had catalytic

  一系列固定有微孔Y沸石（HY，NH 4 Y，NaY）和中孔脱铝DAY沸石（HDAY，HNH 4）的沸石-α-胰凝乳蛋白酶和嗜热菌素DAY），这是首次制备了可在有机溶剂中催化肽键形成的基质。结果表明，大多数固定化沸石的酶对有机介质中的肽合成均具有活性，并且在重复使用五次后仍具有一定程度的催化活性。根据结果​​，Y型微孔沸石的固定化效果优于DAY型中孔沸石，这表明Y型沸石比DAY型沸石具有更多的羟基，因此微孔Y型沸石可以与酶分子形成更强的氢键。 。此外，还研究并优化了反应条件，反应时间和溶剂中的水含量等条件对酶促肽合成的影响。对于两种蛋白酶，NH 4Y沸石没有显示出其对嗜热菌素的优势，但更适合作为固定基质的α-胰凝乳蛋白酶。
• Carbohydrate Protease Conjugates: Stabilized Proteases for Peptide Synthesis
  作者：Charles A. Wartchow、Peng Wang、Mark D. Bednarski、Matthew R. Callstrom

  DOI：10.1021/jo00112a049

  日期：1995.4

  The synthesis of oligopeptides using stable carbohydrate protease conjugates (CPCs) was examined in acetonitrile solvent systems. CPC[alpha-chymotrypsin] was used for the preparation of peptides containing histidine, phenylalanine, tyrosine, and tryptophan in the P-1 position in 60-93% yield. The CPC[alpha-chymotrypsin]-catalyzed synthesis of octamer Z-Gly-Gly-Phe-Gly-Gly-Phe-Gly-Gly-OEt from Z-Gly-Gly-Phe-Gly-Gly-Phe-OMe was achieved in 71% yield demonstrating that synthesis was the dominant kinetic process relative to amide hydrolysis. CPC[papain] was used to synthesize peptides containing both hydrophilic and hydrophobic amino acids. The Pt specificity of papain for aromatic residues was utilized for the 2 + 3 coupling of Z-Tyr-Gly-OMe to H2N-Gly-Phe-Leu-OH to generate the leucine enkephalin derivative in 79% yield. Although papain is nonspecific for the hydrolysis of N-benzyloxycarbonyl amino acid methyl esters in aqueous solution, the rates of synthesis for these derivitives with nucleophile leucine tert-butyl ester differed by nearly 2 orders of magnitude. CPC[thermolysin] was used to prepare the aspartame precursor Z-Asp-Phe-OMe in 90% yield. The increased stability of CPCs prepared from periodate-modified poly(2-methacrylamido-2-deoxy-D-glucose), poly(2-methacrylamido-2-deoxy-D-galactcose) and poly(5-methacrylamido-5-deoxy-D-ribose), carbohydrate materials designed to increase the aldehyde concentration in aqueous solution, suggests that the stability of CPCs is directly related to the aldehyde concentration of the carbohydrate material. Periodate oxidation of poly(2-methacrylamido-2-deoxy-D-glucose) followed by covalent attachment to a-chymotrypsin gave a CPC with catalytic activity in potassium phosphate buffer at 90 degrees C for 2 h.
• The Use of Phosphite Amides in Peptide Syntheses¹
  作者：George W. Anderson、Jack Blodinger、Richard W. Young、Alice D. Welcher

  DOI：10.1021/ja01141a022

  日期：1952.11