O^4.3,O^5.4-diallyl O^1.4-ethyl N^2.1,N^6.1-di-Cbz-L-lysylglycyl-α-L-aspartyl-L-glutamate | 165282-30-4

• 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: O^4.3,O^5.4-diallyl O^1.4-ethyl N^2.1,N^6.1-di-Cbz-L-lysylglycyl-α-L-aspartyl-L-glutamate
• 英文别名: Nα-Cbz-L-Lys(Nζ-Cbz)-Gly-L-Asp(OAll)-L-Glu(OAll)OEt；Cbz-Lys(Cbz)-Gly-Asp(Oallyl)-Glu(Oallyl)-OEt；1-O-ethyl 5-O-prop-2-enyl (2S)-2-[[(2S)-2-[[2-[[(2S)-2,6-bis(phenylmethoxycarbonylamino)hexanoyl]amino]acetyl]amino]-4-oxo-4-prop-2-enoxybutanoyl]amino]pentanedioate
• CAS: 165282-30-4
• 化学式: C₄₁H₅₃N₅O₁₃
• 分子量: 823.898
• InChiKey: YEWIFXAJLPTHKR-ZDCRTTOTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  59
• 可旋转键数：
  32
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.41
• 拓扑面积：
  243
• 氢给体数：
  5
• 氢受体数：
  13

反应信息

• 作为反应物：
  描述：

  O^4.3,O^5.4-diallyl O^1.4-ethyl N^2.1,N^6.1-di-Cbz-L-lysylglycyl-α-L-aspartyl-L-glutamate 在 四(三苯基膦)钯 、 potassium 2-ethylhexanoate 、 N,N-二异丙基乙胺 、 三苯基膦 作用下， 以 乙醇 、 二氯甲烷 、 乙酸乙酯 、 乙腈 为溶剂， 反应 12.0h， 生成 O^5.5-ethyl dihydrogen N^2.1,N^6.1-di-Cbz-L-lysylglycyl-α-L-aspartyl-α-L-glutamyl-α-L-glutamyl-L-seryl-L-leucyl-L-alaninamide
  参考文献：
  名称：

  Gill, Iqbal; López-Fandiño, Rosina; Vulfson, Evgeny, Journal of the American Chemical Society, 1995, vol. 117, # 23, p. 6175 - 6177

  摘要：

  DOI：
• 作为产物：
  描述：

  L-Asp(OAll)OAll 以 乙醇 为溶剂， 反应 42.0h， 生成 O^4.3,O^5.4-diallyl O^1.4-ethyl N^2.1,N^6.1-di-Cbz-L-lysylglycyl-α-L-aspartyl-L-glutamate
  参考文献：
  名称：

  Gill, Iqbal; López-Fandiño, Rosina; Vulfson, Evgeny, Journal of the American Chemical Society, 1995, vol. 117, # 23, p. 6175 - 6177

  摘要：

  DOI：

文献信息

• Pilot-Scale Enzymatic Synthesis of Bioactive Oligopeptides in Eutectic-Based Media
  作者：Iqbal Gill、Rao Valivety

  DOI：10.1021/op025528y

  日期：2002.9.1

  The bioactive peptide precursors N-alpha-Cbz-L-Lys(N-zeta-Cbz)-Gly-OEt (1), N-alpha-Cbz-L-Lys(N-zeta-Cbz)-Gly-L-Asp(OAII)-OAII (2), and N-alpha-Cbz-L-Lys(N-zeta-Cbz)-Gly-L-Asp(OAII)-L-Glu(OAII)OEt (3) were synthesized via a sequential N-to-C strategy in heterogeneous solid-liquid mixtures of substrates using Celite-deposited chymopapain and subtilisin as catalysts. The substrate pairs displayed eutectic formation, and in the presence of 16-20% w/w of water and ethanol furnished low-melting point systems that provided substrate concentrations of 0.81-1.01 M, and sustained protease catalysis. The di-, tri-, and tetra-peptide were obtained in yields of 73, 74, and 67% (yield per step) respectively, and product concentrations of 0.34, 0.48, and 0.45 g per gram of reaction mixture were achieved with these systems. The syntheses were scaled up using wiped-blade and rotating-drum reactors, and 1, 2, and 3 were produced in yields of 71, 73, and 71 %, at product concentrations of 0.36, 0.49, and 0.48 kg kg(-1), on a reaction scale of 11.34, 6.30, and 5.83 kg (11.54, 6.17, and 4.96 mol), respectively. The corresponding space-time yields were 0.30, 0.64, and 0.30 kg kg(-1) d(-1), and biocatalyst reuse provided productivities of 166, 235, and 312 kg-product kg-enzyme(-1). Furthermore, a sequential one-pot, three-step protocol was readily applied to the synthesis of the tetrapeptide 3 which was obtained with an overall yield of 34%, product concentration of 0.25 kg per kg, and space-time yield of 0.07 kg kg(-1) d(-1).
• Gill, Iqbal; López-Fandiño, Rosina; Vulfson, Evgeny, Journal of the American Chemical Society, 1995, vol. 117, # 23, p. 6175 - 6177
  作者：Gill, Iqbal、López-Fandiño, Rosina、Vulfson, Evgeny

  DOI：——

  日期：——