Ac-L-Phe-L-Phe-NH2 | 24809-25-4

• 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: Ac-L-Phe-L-Phe-NH2
• 英文别名: N-Ac-L-Phe-L-Phe-NH2；AcFFNH₂；Ac-Phe-Phe-NH₂；Ac-Phe2-CONH2；Ac-Phe-Phe-NH2；(2S)-2-[[(2S)-2-acetamido-3-phenylpropanoyl]amino]-3-phenylpropanamide
• CAS: 24809-25-4
• 化学式: C₂₀H₂₃N₃O₃
• 分子量: 353.421
• InChiKey: MRIDWVSVNKEVEJ-ROUUACIJSA-N

物化性质

• 沸点：
  730.0±60.0 °C(Predicted)
• 密度：
  1.196±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.9
• 重原子数：
  26
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.25
• 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 Amberlite IR-120 、 18-冠醚-6 、 subtilisin Carlsberg 作用下， 以 乙腈 为溶剂， 生成 Ac-L-Phe-L-Phe-NH2
  参考文献：
  名称：

  Van Unen, Dirk-Jan; Sakodinskaya, Inna K.; Engbersen, Johan F. J., Journal of the Chemical Society. Perkin transactions I, 1998, # 20, p. 3341 - 3343

  摘要：

  DOI：

文献信息

• 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。
• Toward an Optimal Blood−Brain Barrier Shuttle by Synthesis and Evaluation of Peptide Libraries
  作者：Morteza Malakoutikhah、Meritxell Teixidó、Ernest Giralt

  DOI：10.1021/jm800156z

  日期：2008.8.1

  Several peptide families containing N-methylated amino acids were designed and synthesized using solid-phase peptide synthesis (SPPS). The permeability and phospholipophilicity of these compounds were studied by parallel artificial membrane permeability assay (PAMPA) and immobilized artificial membrane chromatography (IAMC) to select the best peptides in terms of length, terminal groups, and amino acid replacement to be used as carriers that pass through a model of the blood-brain barrier (BBB) by passive diffusion. Furthermore, the enzymatic stability of these peptides in human serum and their cell viability by MTT assay were tested. These peptide families showed great stability and nontoxicity. The three peptides that showed the greatest permeability were Coupled to levodopa (a nonpassive permeating drug) and assessed. These peptides effectively transferred levodopa through an artificial membrane by means of passive diffusion.
• Discovery of Dipeptides with High Affinity to the Specific Binding Site for Substance P₁₋₇
  作者：Rebecca Fransson、Milad Botros、Christian Sköld、Fred Nyberg、Gunnar Lindeberg、Mathias Hallberg、Anja Sandström

  DOI：10.1021/jm901352b

  日期：2010.3.25

  Substance P 1-7 (SP1-7, H-Arg-Pro-Lys-Pro-Gln-Gln-Phe-OH) is the major bioactive metabolite of substance P. The interest in this heptapeptide originates from the observation that it modulates, and in certain cases opposes the effects of the parent peptide. e.g., the nociceptive effect. The p-opioid receptor agonist endomorphin-2 (EM-2, H-Tyr-Pro-Phe-Phe-NH2) has been found to also interact with the specific binding site of SP1-7 with only a 10-fold lower affinity compared to the native peptide. Considering the smaller size of EM-2 compared to the target heptapeptide, it was selected as a lead compound in the development of low-molecular-weight ligands to the SP1-7 binding site. An alanine scan and truncation study led to the unexpected discovery of the dipeptide H-Phe-Phe-NH2 (K-i = 1.5 nM), having equal affinity as the endogenous heptapeptide SP1-7. Moreover, the studies show that the C-terminal phenylalanine amide is crucial for the affinity of the dipeptide.
• Peptide synthesis catalyzed by lipases in anhydrous organic solvents
  作者：Alexey L. Margolin、Alexander M. Klibanov

  DOI：10.1021/ja00246a060

  日期：1987.6
• 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.