N-Ac-L-Phe-L-Leu-NH2 | 65118-58-3

• 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-Ac-L-Phe-L-Leu-NH2
• 英文别名: Ac-L-Phe-L-Leu-NH2；Ac-Phe-Leu-NH2；AcPheLeuNH2；N-Acetyl-L-phenylalanyl-L-leucinamide；(2S)-2-[[(2S)-2-acetamido-3-phenylpropanoyl]amino]-4-methylpentanamide
• CAS: 65118-58-3
• 化学式: C₁₇H₂₅N₃O₃
• 分子量: 319.404
• InChiKey: MIBKYCHGORAHFL-GJZGRUSLSA-N

物化性质

• 沸点：
  646.8±55.0 °C(Predicted)
• 密度：
  1.122±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  23
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  101
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-Ac-L-Phe-L-Leu-NH2 生成 L-Phe-L-Leu-NH2
  参考文献：
  名称：

  Incorporation of D-amino acids into peptides via enzymic condensation in organic solvents

  摘要：

  DOI：

  10.1021/ja00259a049
• 作为产物：
  描述：

  亮氨酰胺 、 L-苯丙氨酸,N-乙酰基-,2-氯乙基酯 在 endopeptidase So 作用下， 以 2-甲基-2-丁醇 为溶剂， 反应 96.0h， 生成 N-Ac-L-Phe-L-Leu-NH2
  参考文献：
  名称：

  Incorporation of D-amino acids into peptides via enzymic condensation in organic solvents

  摘要：

  DOI：

  10.1021/ja00259a049

文献信息

• Peptide synthesis mediated by immobilized and viable baker's yeast in reverse micelles: synthesis of leucine enkephalin analogues
  作者：N. W. Fadnavis、A. Deshpande、S. Chauhan、U. T. Bhalerao

  DOI：10.1039/c39900001548

  日期：——

  Cells of baker's yeast (Saccharomyces cerevisiaeNCIM 3305) immobilized in calcium alginate beads are found to be viable in reverse micelles of bis(2-ethylhexyl)sulphosuccinate sodium salt 1 in iso-octane for days and were used for the first time for peptide synthesis (in aerosol OT reverse micelles) using hydrophobic substrates.

  发现固定在海藻酸钙珠粒中的面包酵母（Saccharomyces cerevisiae NCIM 3305）细胞在异辛烷中的双（2-乙基己基）磺基琥珀酸钠盐1的反胶束中可存活数天，并首次用于肽合成（在气溶胶OT反胶束中）使用疏水性底物。
• 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。
• Competition between model protocells driven by an encapsulated catalyst
  作者：Katarzyna Adamala、Jack W. Szostak

  DOI：10.1038/nchem.1650

  日期：2013.6

  The advent of Darwinian evolution required the emergence of molecular mechanisms for the heritable variation of fitness. One model for such a system involves competing protocell populations, each consisting of a replicating genetic polymer within a replicating vesicle. In this model, each genetic polymer imparts a selective advantage to its protocell by, for example, coding for a catalyst that generates a useful metabolite. Here, we report a partial model of such nascent evolutionary traits in a system that consists of fatty-acid vesicles containing a dipeptide catalyst, which catalyses the formation of a second dipeptide. The newly formed dipeptide binds to vesicle membranes, which imparts enhanced affinity for fatty acids and thus promotes vesicle growth. The catalysed dipeptide synthesis proceeds with higher efficiency in vesicles than in free solution, which further enhances fitness. Our observations suggest that, in a replicating protocell with an RNA genome, ribozyme-catalysed peptide synthesis might have been sufficient to initiate Darwinian evolution. Darwinian evolution involves competition between members of a population. Here, the synthesis of a hydrophobic dipeptide catalysed by a second dipeptide in a model protocell — a vesicle — is described. The reaction product partitions to the vesicle membrane, which grows by accumulating fatty acids derived from neighbouring vesicles. Thus, an encapsulated catalyst drives competition between the model protocells.

  达尔文进化论的出现，要求出现适应性遗传变异的分子机制。这种系统的一种模式涉及相互竞争的原细胞群，每个原细胞群由复制囊泡中的复制基因聚合物组成。在这一模型中，每种基因聚合物通过编码产生有用代谢物的催化剂等方式，为其原细胞带来选择性优势。在这里，我们报告了这种新生进化性状的部分模型，该系统由含有二肽催化剂的脂肪酸囊泡组成，二肽催化剂可催化第二种二肽的形成。新形成的二肽与囊泡膜结合，增强了对脂肪酸的亲和力，从而促进了囊泡的生长。与自由溶液相比，二肽在囊泡中的催化合成效率更高，从而进一步提高了适应性。我们的观察结果表明，在具有 RNA 基因组的复制原细胞中，核糖酶催化的肽合成可能足以启动达尔文进化论。达尔文进化涉及种群成员之间的竞争。本文描述了一个疏水二肽在模型原细胞 "囊泡 "中由第二个二肽催化合成的过程。反应产物分化到囊泡膜上，囊泡膜通过积聚来自邻近囊泡的脂肪酸而生长。因此，封装催化剂推动了模型原细胞之间的竞争。
• Novel peptide-forming enzyme gene
  申请人：Ajinomoto Co., Inc.

  公开号：US20040204577A1

  公开（公告）日：2004-10-14

  DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

  本文揭示了编码肽形成酶的DNA和重组DNA，生产肽形成酶的方法，以及生产二肽的方法。生产二肽的方法包括使用属于拟杆菌属的微生物培养物，并具有从羧基组分和胺基组分形成二肽的能力，从培养物中分离的微生物细胞，经处理的微生物细胞产物或源自该微生物的肽形成酶，来从羧基组分和胺基组分中生产二肽。
• Method for producing tripeptides and/or peptides longer than tripeptides
  申请人：Ajinomoto Co., Inc.

  公开号：US20040219631A1

  公开（公告）日：2004-11-04

  A method is disclosed that allows the production of peptides having three or more amino acid residues easily, inexpensively and at high yield without going through a complex synthesis method. A novel enzyme that efficiently produces a peptide from bacteria belonging to the genus Empedobacter or the genus Sphingobacterium is provided. The enzyme acts on a carboxy component and an amine component to form peptides having three or more amino acid residues by acting on a carboxy component and an amine component.

  本发明揭示了一种方法，可以在不经过复杂的合成方法的情况下，轻松、廉价、高产地生产具有三个或更多氨基酸残基的肽。提供了一种从属于Empedobacter属或Sphingobacterium属的细菌中高效产生肽的新型酶。该酶通过作用于羧基组分和胺基组分来形成具有三个或更多氨基酸残基的肽。