Z-Ala-Phe-Leu-OH | 79113-78-3

• 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: Z-Ala-Phe-Leu-OH
• CAS: 79113-78-3
• 化学式: C₂₆H₃₃N₃O₆
• 分子量: 483.565
• InChiKey: LALHBVLRQZWPLW-NYVOZVTQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.64
• 重原子数：
  35.0
• 可旋转键数：
  12.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  133.83
• 氢给体数：
  4.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  L-亮氨酸甲酯盐酸盐 、 Z-Ala-Phe-Leu-OH 在 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 1,4-二氧六环 为溶剂， 反应 4.0h， 以147 mg的产率得到Cbz-Ala-Phe-Leu-Leu-OMe
  参考文献：
  名称：

  A One-Pot Saponification–Coupling Sequence Suitable for C-Terminus Peptide Elongation Using Lithium Carboxylates

  摘要：

  DOI：

  10.1055/s-0034-1378330
• 作为产物：
  描述：

  (S)-2-((S)-2-Benzyloxycarbonylamino-propionylamino)-3-phenyl-propionic acid methyl ester 在 水 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 、 lithium hydroxide 作用下， 以 1,4-二氧六环 为溶剂， 反应 10.0h， 生成 Z-Ala-Phe-Leu-OH
  参考文献：
  名称：

  A One-Pot Saponification–Coupling Sequence Suitable for C-Terminus Peptide Elongation Using Lithium Carboxylates

  摘要：

  DOI：

  10.1055/s-0034-1378330

文献信息

• Facile Amide Bond Formation From Esters of Amino Acids and Peptides Catalyzed by Alkaline Protease in Anhydrous<i>tert</i>-Butyl Alcohol Using Ammonium Chloride/Triethylamine as a Source of Nucleophilic Ammonia
  作者：Shui-Tein Chen、Ming-Kuei Jang、Kung-Tsung Wang

  DOI：10.1055/s-1993-25955

  日期：——

  An industrial alkaline protease "Alcalase", stable and active in tert-butyl alcohol, was used to catalyze the synthesis of N-protected amino acids or peptide amides in anhydrous tert-butyl alcohol using ammonium chloride/triethylamine as source of nucleophilic ammonia

  一种工业碱性蛋白酶 "Alcalase"，其在叔丁醇中稳定且具有活性，被用于在无水叔丁醇中使用氯化铵/三乙胺作为亲核氨源，催化合成 N-保护氨基酸或肽酰胺。
• Tandem deprotection/coupling for peptide synthesis in water at room temperature
  作者：Margery Cortes-Clerget、Jean-Yves Berthon、Isabelle Krolikiewicz-Renimel、Laurent Chaisemartin、Bruce H. Lipshutz

  DOI：10.1039/c7gc01575e

  日期：——

  A tandem deprotection/coupling sequence is reported for solution-phase peptide synthesis in water under micellar catalysis conditions using the designer surfactant TPGS-750-M. Cbz deprotection followed by peptide coupling in the presence of COMU and 2,6-lutidine afforded polypeptides containing up to 10 amino acid residues. A broad scope characterizes this new technology. No epimerization has been

  据报道，在使用胶束表面活性剂TPGS-750-M的胶束催化条件下，溶液相肽在水中的合成过程中，串联脱保护/偶联序列。Cbz脱保护，然后在COMU和2,6-lutidine存在下进行肽偶联，得到的多肽含有多达10个氨基酸残基。这项新技术的广泛应用。未检测到差向异构。由于“逐步经济”和产品提取所需的有机溶剂量最少，相关的E因子（作为“绿色度”的一种度量标准，已知对肽偶联的影响非常高）已减少至小于10。
• Enzyme-catalyzed peptide synthesis in biphasic aqueous-organic systems
  作者：P. Kuhl、A. Könnecke、G. Döring、H. Däumer、N.-D. Jakubke

  DOI：10.1016/s0040-4039(00)77731-8

  日期：1980.1

  A preparative protease-catalyzed peptide synthesis in biphasic aqueous-organic systems is described. This approach using both free as well as immobilized proteases as catalysts provides high yields and includes the possibility to re-utilize the enzymes.

  描述了在双相水-有机系统中制备蛋白酶催化的肽合成。使用游离的和固定的蛋白酶作为催化剂的这种方法提供了高产率，并且包括重新利用酶的可能性。
• 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.