Fmoc-Asp(SH)-Leu-OMe | 1262658-19-4

• 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: Fmoc-Asp(SH)-Leu-OMe
• 英文别名: (3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-4-[[(2S)-1-methoxy-4-methyl-1-oxopentan-2-yl]amino]-4-oxobutanethioic S-acid
• CAS: 1262658-19-4
• 化学式: C₂₆H₃₀N₂O₆S
• 分子量: 498.6
• InChiKey: SGKDKZXVAFWWHU-VXKWHMMOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.1
• 重原子数：
  35
• 可旋转键数：
  12
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  112
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Fmoc-Asp(SH)-Leu-OMe 、 N,N'-diacetylchitobiosamine 在 1-羟基苯并三唑 作用下， 以 二甲基亚砜 为溶剂， 反应 12.0h， 以84%的产率得到methyl (2S)-2-[[(2S)-4-[[(2R,3R,4R,5S,6R)-3-acetamido-5-[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4-hydroxy-6-(hydroxymethyl)oxan-2-yl]amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-oxobutanoyl]amino]-4-methylpentanoate
  参考文献：
  名称：

  Encouraging Progress in the ω-Aspartylation of Complex Oligosaccharides as a General Route to β-N-Linked Glycopolypeptides

  摘要：

  Described herein is a method for the joining of complex peptides to complex oligosaccharides via an N-linkage. The omega-aspartylation is conducted by coupling fully deprotected glycosylamine with a peptide containing a unique thioacid at the omega-aspartate carboxyl. In the presence of HOBT, under conditions that, in principle, allow for oxidation, complex components are combined in encouraging yields to produce structurally and stereochemically defined N-linked glycopolypeptides wherein the carbohydrate domain can be quite complex. Various mechanisms for oxidative coupling are proposed.

  DOI：

  10.1021/ja110115a

文献信息

• Encouraging Progress in the ω-Aspartylation of Complex Oligosaccharides as a General Route to β-N-Linked Glycopolypeptides
  作者：Ping Wang、Xuechen Li、Jianglong Zhu、Jin Chen、Yu Yuan、Xiangyang Wu、Samuel J. Danishefsky

  DOI：10.1021/ja110115a

  日期：2011.2.9

  Described herein is a method for the joining of complex peptides to complex oligosaccharides via an N-linkage. The omega-aspartylation is conducted by coupling fully deprotected glycosylamine with a peptide containing a unique thioacid at the omega-aspartate carboxyl. In the presence of HOBT, under conditions that, in principle, allow for oxidation, complex components are combined in encouraging yields to produce structurally and stereochemically defined N-linked glycopolypeptides wherein the carbohydrate domain can be quite complex. Various mechanisms for oxidative coupling are proposed.