Z-Ala-Ala-Leu-OCH3 | 63276-80-2

• 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-Ala-Leu-OCH3
• 英文别名: Z-Ala-Ala-Leu-OMe；Cbz-Ala-Ala-Leu-OMe；Z-Ala-Ala-Leu-O-Me；methyl (2S)-4-methyl-2-[[(2S)-2-[[(2S)-2-(phenylmethoxycarbonylamino)propanoyl]amino]propanoyl]amino]pentanoate
• CAS: 63276-80-2
• 化学式: C₂₁H₃₁N₃O₆
• 分子量: 421.494
• InChiKey: JSXGZEKJONDZNE-ZOBUZTSGSA-N

物化性质

• 沸点：
  643.3±55.0 °C(Predicted)
• 密度：
  1.151±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  30
• 可旋转键数：
  12
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  123
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  Z-Ala-Ala-Leu-OCH3 在 silochrom 、 subtilisin 72 作用下， 以 乙酸酐 、 二甲基亚砜 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 4.0h， 生成 Z-Ala-Ala-Leu-Pheal
  参考文献：
  名称：

  Enzymatic synthesis of peptidyl amino alcohols and peptidyl amino aldehydes-serine proteinase inhibitors

  摘要：

  An enzymatic synthesis of peptidyl amino alcohols is described. The reactions were performed in organic solvents using as a catalyst subtilisin distributed on the surface of macroporous silica. Subsequent mild oxidation of peptidyl amino alcohols results in peptide aldehydes - the potent specific inhibitors of serine proteinases. (C) 1997 Elsevier Science Ltd.

  DOI：

  10.1016/s0960-894x(97)00091-7
• 作为产物：
  描述：

  (2S)-2-氨基-4-甲基戊酸甲酯 、 N-(苄氧羰基)-L-丙氨酰-L-丙氨酸 在 Tris-HCl buffer 、 calcium chloride 作用下， 以 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 24.0h， 以33%的产率得到Z-Ala-Ala-Leu-OCH3
  参考文献：
  名称：

  Biocatalytic properties of thermolysin immobilized on polyvinyl alcohol cryogel

  摘要：

  Preparations with different contents of thermolysin were obtained by the immobilization of the enzyme on granulated polyvinyl alcohol cryogel. Their activity and stability in an aqueous medium and in mixtures of polar organic solvents of different composition were investigated. The catalytic properties of the preparations in reactions of peptide bond formation were studied, and the optimal amount of the biocatalyst, the concentrations of initial reagents, and the ratios of organic solvents and water necessary for effective enzymatic peptide synthesis catalyzed by immobilized thermolysin were determined. A series of peptides of the general formula Z-Ala-Ala-Xaa-pNA, where Xaa = Leu, Ile, Phe, Val, or Ala, were synthesized, and the immobilized enzyme was shown to retain substrate specificity in an organic medium.

  DOI：

  10.1134/s1068162008040079

文献信息

• Synthesis of peptide aldehydes via enzymatic acylation of amino aldehyde derivatives
  作者：Tatiana L. Voyushina、Joanna V. Potetinova、Ekaterina I. Milgotina、Valentin M. Stepanov

  DOI：10.1016/s0968-0896(99)00237-0

  日期：1999.12

  Two ways for semi-enzymatic preparation of the peptide aldehydes are proposed: (1) enzymatic acylation of amino alcohols with acyl peptide esters and subsequent chemical oxidation of the resulting peptide alcohols with DMSO/acetic anhydride mixture or (2) enzymatic acylation of the preliminarily obtained by a chemical route amino aldehyde semicarbazones. Subtilisin 72, serine proteinase with a broad

  提出了两种半酶法制备肽醛的方法：（1）将氨基醇与酰基肽酯进行酶促酰化，然后将所得的肽醇与DMSO /乙酸酐混合物进行化学氧化，或（2）将酶进行初步的酰化。通过化学途径获得的氨基醛半咔唑。在两种情况下，枯草杆菌蛋白酶72（一种广泛的丝氨酸蛋白酶）均分布在大孔硅胶上，被用作催化剂。由于反应混合物中实际上没有水，所以两种酶促反应中产物的收率几乎都是定量的。第二种方法似乎更具吸引力，因为所有化学步骤均使用氨基酸衍生物进行，而氨基酸衍生物的价值远低于肽化合物。获得了一系列通式为Z-Ala-Ala-Xaa-al的肽醛（其中Xaa-al ＝亮氨酸，苯丙氨酸，丙氨酸，缬氨酸）。在枯草杆菌蛋白酶和α-胰凝乳蛋白酶的相应生色底物的水解反应中，确定了这些化合物的抑制参数。
• Peptide Synthesis in Organic Media with the Use of Subtilisin 72 Immobilized on a Poly(Vinyl Alcohol) Cryogel
  作者：A. V. Belyaeva、A. V. Bacheva、E. S. Oksenoit、E. N. Lysogorskaya、V. I. Lozinskii、I. Yu. Filippova

  DOI：10.1007/s11171-005-0072-y

  日期：2005.11

  Subtilisin 72 serine protease (EC 3.4.21.14) immobilized on a poly(vinyl alcohol) cryogel was used as a catalyst in the syntheses of N-protected peptide p-nitroanilides of the general formulas Z(or Boc)-Xaa-Phe-pNA (Xaa = Leu or Ala), Z-Ala-Xaa-Yaa-pNA (Xaa = Leu or Ala; Yaa = Leu or Phe), and Z-Ala-Ala-Xaa-Yaa-pNA (Xaa = Leu, Arg, or Gly; Yaa = Phe, Leu, Gly, Asp, or Glu). The syntheses were carried out in DMF-acetonitrile mixtures. A number of protected di-, tri-, and tetrapeptides were prepared in yields up to 99%. The syntheses were found to retain stereoselectivity under the conditions studied. The activation of carboxyl group of the acylating component was shown to have a positive effect upon the coupling rate.

  将固定于聚乙烯醇冻胶上的72丝氨酸蛋白酶（EC 3.4.21.14）用作合成N-保护肽对硝基苯胺的催化剂，其通式为Z（或Boc）-Xaa-Phe-pNA（Xaa=亮氨酸或丙氨酸）、Z-Ala-Xaa-Yaa-pNA（Xaa=亮氨酸或丙氨酸；Yaa=亮氨酸或苯丙氨酸）和Z-Ala-Ala-Xaa-Yaa-pNA（Xaa=亮氨酸、精氨酸或甘氨酸；Yaa=苯丙氨酸、亮氨酸、甘氨酸、天冬氨酸或谷氨酸）。合成在DMF-乙腈混合物中进行。制备了一系列二肽、三肽和四肽保护物，收率高达99%。研究发现，在所研究的条件下，合成保留了立体选择性。酰化成分羧基的活化对偶联率有积极影响。
• ——
  作者：A. V. Bacheva、O. V. Baibak、A. V. Belyaeva、E. N. Lysogorskaya、E. S. Oksenoit、V. I. Lozinskii、I. Yu. Filippova

  DOI：10.1023/a:1026013912147

  日期：——

  that of the native subtilisin. The use of N-acylpeptides with a free carboxyl group was found to be possible in organic solvents during the enzymatic synthesis catalyzed by both native and immobilized subtilisin. A series of tetrapeptide p-nitroanilides of the general formula Z-Ala-Ala-Xaa-Yaa-pNA (where Xaa is Leu, or Glu and Yaa is Phe or Asp) was obtained in the presence of immobilized enzyme in yields

  在低水含量的有机溶剂混合物中，取决于介质的组成，研究了肽偶联反应中天然枯草杆菌蛋白酶，其与聚丙烯酸酯的非共价复合物以及共价固定在聚乙烯醇冷冻凝胶中的枯草杆菌蛋白酶的催化效率，反应时间和生物催化剂浓度。已经确定，在DMF含量＞ 80％的培养基中，修饰的枯草杆菌蛋白酶的合酶活性高于天然枯草杆菌蛋白酶的合酶活性。发现在天然和固定的枯草杆菌蛋白酶催化的酶促合成过程中，可以在有机溶剂中使用具有游离羧基的N-酰基肽。一系列通式为Z-Ala-Ala-Xaa-Yaa-pNA的四肽对硝基苯胺（其中Xaa是Leu，
• Biocomposite of subtilisin Carlsberg with chitosan as an effective biocatalyst for hydrolysis and synthesis of peptides
  作者：A. V. Bacheva、M. S. Isakov、E. N. Lysogorskaya、D. J. Macquarrie、I. Yu. Philippova

  DOI：10.1134/s106816200803014x

  日期：2008.5

  obtained. The enzyme content, hydrolytic activity, and ability to catalyze peptide bond formation in organic solvents were characterized for these preparations. The influence of the form and composition of the biocomplosite (content of the enzyme and glutaraldehyde, the cross-linking agent) and buffer pH on the biocatalytic properties of the immobilized enzyme was studied in the reactions of peptide bond

  获得了新的生物催化剂，即固定在壳聚糖（甲壳素的脱乙酰衍生物）上的嘉士伯枯草杆菌蛋白酶制剂。对这些制剂的酶含量、水解活性和在有机溶剂中催化肽键形成的能力进行了表征。在肽键水解反应中研究了生物复合材料的形式和组成（酶和戊二醛、交联剂的含量）和缓冲液的pH值对固定化酶的生物催化性能的影响。在 Z-Ala-Ala-Leu-Phe-pNA 在 6:4 DMF-乙腈混合物中的合成反应中，根据反应时间研究了制剂的合酶活性。仅40分钟后该产物的产率为100%。
• ——
  作者：I. Yu. Filippova、E. N. Lysogorskaya

  DOI：10.1023/a:1026061828077

  日期：——

  proteases could catalyze synthesis of a wide variety of peptides of various lengths and structures both in solution and on solid phase in organic solvents. The following modified proteases were studied as catalysts for enzymatic peptide synthesis in polar organic solvents (acetonitrile, dimethylformamide, and ethanol): pepsin sorbed on celite, a noncovalent complex of subtilisin with sodium dodecylsulfate

  我们表明，修饰的蛋白酶可以在有机溶剂中的溶液和固相上催化各种长度和结构各异的肽的合成。研究了以下修饰的蛋白酶，作为在极性有机溶剂（乙腈，二甲基甲酰胺和乙醇）中酶促肽合成的催化剂：吸附在硅藻土上的胃蛋白酶，枯草杆菌蛋白酶与十二烷基硫酸钠的非共价复合物，以及枯草杆菌蛋白酶或嗜热菌蛋白酶共价固定在聚乙烯基冷冻凝胶上醇。枯草杆菌蛋白酶与十二烷基硫酸钠和固定的枯草杆菌蛋白酶的非共价复合物的使用对于多肽片段的片段缩合特别有希望，该片段包含侧链中带有未保护离子源基团的三官能氨基酸残基，例如Lys，Arg，His，Glu和Asp 。