N-(N-acetyl-L-phenylalaninyl)glycinamide | 29701-43-7

• 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: N-(N-acetyl-L-phenylalaninyl)glycinamide
• 英文别名: N-(N-acetyl-L-phenylalanyl)glycinamide；N-acetyl-phenylalanine-glycinamide；N-acetylphenylalanineglycinamide；Ac-Phe-Gly-NH2；N-Ac-Phe-Gly-NH2；Glycinamide, N-acetyl-L-phenylalanyl-；(2S)-2-acetamido-N-(2-amino-2-oxoethyl)-3-phenylpropanamide
• CAS: 29701-43-7
• 化学式: C₁₃H₁₇N₃O₃
• 分子量: 263.296
• InChiKey: SIWSILBKWOOCLY-NSHDSACASA-N

物化性质

• 沸点：
  665.9±55.0 °C(Predicted)
• 密度：
  1.208±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.5
• 重原子数：
  19
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  101
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  N-乙酰-L-苯丙氨酸 在 N-甲基吗啉 、 氨 作用下， 以 四氢呋喃 为溶剂， 反应 15.83h， 生成 N-(N-acetyl-L-phenylalaninyl)glycinamide
  参考文献：
  名称：

  羧基修饰的氨基酸和肽作为蛋白酶抑制剂。

  摘要：

  制备几种类型的羧基修饰的氨基酸和肽，它们具有适合于几种代表性蛋白酶之一的N末端修饰（载体片段），并评估了它们对这些酶的抑制作用。羧基修饰（抑制单元）包括（b）CONH 2，（c）CSNH 2，（d）CN，（e）反式-CH ＝ CHCO 2 Me和（f）反式-CH ＝ CHSO 2 Me。载体片段包括NH2（PhCH2）CHX（1），AcNH（PhCH2）CHX（2），H2NCH2CONH（PhCH2）CHX（3）和AcNH（PhCH2）CHCONHCH2X（4）。化合物1b，1d，1e和1f是微粒体和胞质亮氨酸氨基肽酶的竞争性抑制剂（前者的Ki分别为14.8、67、61和3.7 mM，后者分别为14.1、26.4、27.3和8.8 mM） 。化合物1c和亮氨酸硫代酰胺均对这两种酶均无任何可检测的作用。化合物2b-f还是胰凝乳蛋白酶的竞争性抑制剂（Ki分别为13.9、23.0、5.3、30.8和29

  DOI：

  10.1021/jm00151a018

文献信息

• Chymotrypsin-Catalyzed Peptide Synthesis in Deep Eutectic Solvents
  作者：Zaira Maugeri、Walter Leitner、Pablo Domínguez de María

  DOI：10.1002/ejoc.201300448

  日期：2013.7

  formed by mixing quaternary ammonium salts (e.g., choline chloride) and hydrogen-bond donors (e.g., glycerol or urea), which leads to biodegradable and readily available ionic solvents at room temperature. Analogous to other ionic liquids, DESs represent a promising reaction media if hydrophobic and hydrophilic substrates need to be combined. This paper assesses DESs as reaction media for chymotrypsin-catalyzed

  深共熔溶剂 (DES) 是通过混合季铵盐（例如氯化胆碱）和氢键供体（例如甘油或尿素）形成的，这导致在室温下可生物降解且易于获得的离子溶剂。与其他离子液体类似，如果需要结合疏水和亲水底物，DESs 是一种很有前途的反应介质。本文评估了 DES 作为糜蛋白酶催化肽合成的反应介质。在仔细确定反应条件（例如，水含量、酶加载量）后，α-胰凝乳蛋白酶在氯化胆碱/甘油混合物中显示出对肽合成的高活性，可提供约 10 倍的产率。20 g L–1 h–1 并且对肽具有完全选择性，这与在水性介质中观察到的有害水解途径相反。非固定化悬浮酶可以通过简单的过滤重复使用多次，具有优异到中等的活性。总体而言，报告的结果表明，基于氯化胆碱的 DES 可能成为通过生物催化合成肽的有前途的新型溶剂。
• Optimal α-Chymotrypsin-Catalyzed Synthesis of <i>N</i>-Ac-Phe-Gly-NH₂
  作者：Hen-Yi Ju、Jui-Rze Too、Cheng Chang、Chwen-Jen Shieh

  DOI：10.1021/jf802103s

  日期：2009.1.28

  N-Acetyl-phenylalanine-glycinamide (N-Ac-Phe-Gly-NH2), a type of dipeptide derivative, was synthesized from N-acetyl phenylalanine ethyl ester and glycinamide and catalyzed by α-chymotrypsin, a protease, in a biphasic system. Response surface methodology with a four-factor, five-level central composite rotatable design was employed to evaluate the effects of selected parameters that included incubation

  N-乙酰基苯丙氨酸-甘氨酰胺（N -Ac-Phe-Gly-NH 2）是一种二肽衍生物，由N-乙酰基苯丙氨酸乙酯和甘氨酰胺合成，并被蛋白酶α-胰凝乳蛋白酶催化。系统。采用具有四因子，五级中心复合材料可旋转设计的响应面方法，评估了所选参数的影响，包括孵育时间，反应温度，酶活性和pH值对二肽衍生物收率的影响。结果表明，pH显着影响N -Ac-Phe-Gly-NH 2的产率。在最大峰分析中，该合成的最佳条件包括30.9分钟的孵育时间，35.8°C的反应温度，159.2 U的酶活性和8.98的pH。预测的和实际的（实验）产率分别为98.0％和95.1％。
• Optimal covalent immobilization of α-chymotrypsin on Fe3O4-chitosan nanoparticles
  作者：Hen-Yi Ju、Chia-Hung Kuo、Jui-Rze Too、Hsin-Yi Huang、Yawo-Kuo Twu、Chieh-Ming J. Chang、Yung-Chuan Liu、Chwen-Jen Shieh

  DOI：10.1016/j.molcatb.2012.01.015

  日期：2012.6

  This study investigated the immobilization of alpha-chymotrypsin onto magnetic Fe3O4-chitosan (alpha-chymotrypsin-Fe3O4-CS) nanoparticles by covalent binding. The response surface methodology (RSM) with a 3-factor-3-level Box-Behnken experimental design was employed to evaluate the effects of the manipulated variables, including the immobilization time, temperature, and pH, on the enzyme activity. The results indicate that the immobilized temperature and pH significantly affected enzyme activity. In a ridge max analysis, the optimal condition for alpha-chymotrypsin immobilization included a reaction temperature of 21.7 degrees C, a pH of 7.6, and an incubation time of 1.1 h. The predicted and the experimental immobilized enzyme activities were 354 and 347 +/- 46.5 U/g-support, respectively, under the optimal condition. Besides, the synthesis reactions of the dipeptide derivative using the free and immobilized alpha-chymotrypsin were compared. The yields of the dipepticle derivative via the free or immobilized alpha-chymotrypsin catalyzed were almost the same. The alpha-chymotrypsin-Fe3O4-CS nanoparticles exhibited a good acid-resisting ability and the less reaction time was required for dipeptide synthesis. After twelve repeated uses in dipeptide synthesis, the immobilized alpha-chymotrypsin still retained over 60% of its original activity. The magnetic alpha-chymotrypsin-Fe3O4-CS nanoparticles can be easily recovered by magnetic field will have potential application in industry. (C) 2012 Elsevier By. All rights reserved.