Cbz-Ala-Phe-Ala-NH2 | 65356-79-8

• 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: Cbz-Ala-Phe-Ala-NH2
• 英文别名: benzyl N-[(2S)-1-[[(2S)-1-[[(2S)-1-amino-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxopropan-2-yl]carbamate
• CAS: 65356-79-8
• 化学式: C₂₃H₂₈N₄O₅
• 分子量: 440.499
• InChiKey: WWZFWDYPDJWMCF-BXWFABGCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  32
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  140
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  (S)-2-((S)-2-Benzyloxycarbonylamino-propionylamino)-3-phenyl-propionic acid methyl ester 、 L-丙氨酰胺盐酸盐 在 Alcalase 作用下， 以 2-甲基-2-丁醇 为溶剂， 反应 72.0h， 以87%的产率得到Cbz-Ala-Phe-Ala-NH2
  参考文献：
  名称：

  Chemo-Enzymatic Synthesis of Optically Active Amino Acids and Peptides

  摘要：

  AbstractThe industrial alkaline protease, alcalase, is stable and active in a high concentration of organic solvents and useful as a biocatalyst for (i) diastereoselective hydrolysis of peptide esters and preparation of racemization‐free peptides; (ii) selective incorporation of esters of D‐amino acid into peptides in t‐butanol via a selective hydrolysis of esters of D,L‐amino acid, followed by using the unhydrolyzed D‐esters as a nucleophile in a kinetically controlled peptide bond formation; (iii) resolution of esters of amino acid in 95% t‐butanol/5% water, followed by saponification of the unreacted esters to offer both enantiomers with high yield and optical purity; (iv) completely resolve amino‐acid esters with high yield and optical purity via in situ racemization of the unreacted antipode catalyzed by pyridoxal 5‐phosphate; (v) cryobioorganic synthesis of peptides with increased yields 15%–40% of peptide bond formation by reaction at 5 °C instead of 25–30 °C of a kinetically controlled enzymatic reaction in alcohols.

  DOI：

  10.1002/jccs.199900046

文献信息

• Kinetically controlled peptide bond formation in anhydrous alcohol catalyzed by the industrial protease alcalase
  作者：Shui Tein Chen、Shiah Yun Chen、Kung Tsung Wang

  DOI：10.1021/jo00051a052

  日期：1992.12

  The industrial alkaline protease alcalase has been found to be very stable (half life > 5 days in ethanol or 2-methyl-2-propanol) and active in alcoholic solvents (except methanol). Procedures have been developed for alcalase-catalyzed, kinetically controlled peptide bond formation in anhydrous alcohol(ethanol, 2-methyl-2-propanol). Studies of the selectivity of an alcalase-catalyzed reaction show that only L-amino acid acyl donors are substrates at the p-1 subsite of alcalase; at the p-1' subsite both D- and L-amino acid nucleophiles are substrates. Other amino compounds such as benzylamine and phenylhydrazine are good nucleophiles. Studies of the effect of the water content of the reaction solution on the yield in the synthesis of Moz-Phe-Leu-NH2 showed that the 95% yield obtained in anhydrous 2-methyl-2-propanol was decreased to 48% in 2-methyl-2-propanol containing 4.86% water.
• Chemo-Enzymatic Synthesis of Optically Active Amino Acids and Peptides
  作者：Shui-Tein Chen、Kung-Tsung Wang

  DOI：10.1002/jccs.199900046

  日期：1999.6

  AbstractThe industrial alkaline protease, alcalase, is stable and active in a high concentration of organic solvents and useful as a biocatalyst for (i) diastereoselective hydrolysis of peptide esters and preparation of racemization‐free peptides; (ii) selective incorporation of esters of D‐amino acid into peptides in t‐butanol via a selective hydrolysis of esters of D,L‐amino acid, followed by using the unhydrolyzed D‐esters as a nucleophile in a kinetically controlled peptide bond formation; (iii) resolution of esters of amino acid in 95% t‐butanol/5% water, followed by saponification of the unreacted esters to offer both enantiomers with high yield and optical purity; (iv) completely resolve amino‐acid esters with high yield and optical purity via in situ racemization of the unreacted antipode catalyzed by pyridoxal 5‐phosphate; (v) cryobioorganic synthesis of peptides with increased yields 15%–40% of peptide bond formation by reaction at 5 °C instead of 25–30 °C of a kinetically controlled enzymatic reaction in alcohols.