N-acetyl glycyltryptophan ethyl ester

• 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: N-acetyl glycyltryptophan ethyl ester
• 英文别名: ethyl (2S)-2-[(2-acetamidoacetyl)amino]-3-(1H-indol-3-yl)propanoate
• 化学式: C₁₇H₂₁N₃O₄
• 分子量: 331.371
• InChiKey: OSLMBHQGRIHGQK-HNNXBMFYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  24
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  100
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-acetyl glycyltryptophan ethyl ester 在 三氟乙酸 作用下， 反应 12.0h， 以72%的产率得到(S)-2-(2-Acetylamino-acetylamino)-3-{3'-[(S)-2-(2-acetylamino-acetylamino)-2-ethoxycarbonyl-ethyl]-2,3-dihydro-1H,1'H-[2,2']biindolyl-3-yl}-propionic acid ethyl ester
  参考文献：
  名称：

  The retro-mannich cleavage of δ 1 ,δ 1 ′-tryptophan dimers

  摘要：

  Under acidic conditions tryptophan sidechains crosslink to form delta(1), delta(1)'-tryptophan dimers through a Mannich-type mechanism. Tryptophan dimers are readily cleaved at high temperatures under acidic conditions making it impossible to isolate tryptophan dimers under standard conditions of acidic protein hydrolysis. In a prescriptive sense this cleavage can be used to recover peptides that have undergone tryptophan crosslinking, although the yields drop with increasing peptide length due to competitive cleavage of the amide bonds. The best conditions for cleavage involve ting the dimeric peptides in dilute ethanolic HCl at 150 degrees C in the presence of ten equivalents of ethanedithiol. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(98)00071-6
• 作为产物：
  描述：

  (S)-2-(2-Acetylamino-acetylamino)-3-{3'-[(S)-2-(2-acetylamino-acetylamino)-2-ethoxycarbonyl-ethyl]-2,3-dihydro-1H,1'H-[2,2']biindolyl-3-yl}-propionic acid ethyl ester 在 盐酸 、 ethandithiol 作用下， 以 乙醇 为溶剂， 反应 1.5h， 以40%的产率得到N-acetyl glycyltryptophan ethyl ester
  参考文献：
  名称：

  The retro-mannich cleavage of δ 1 ,δ 1 ′-tryptophan dimers

  摘要：

  Under acidic conditions tryptophan sidechains crosslink to form delta(1), delta(1)'-tryptophan dimers through a Mannich-type mechanism. Tryptophan dimers are readily cleaved at high temperatures under acidic conditions making it impossible to isolate tryptophan dimers under standard conditions of acidic protein hydrolysis. In a prescriptive sense this cleavage can be used to recover peptides that have undergone tryptophan crosslinking, although the yields drop with increasing peptide length due to competitive cleavage of the amide bonds. The best conditions for cleavage involve ting the dimeric peptides in dilute ethanolic HCl at 150 degrees C in the presence of ten equivalents of ethanedithiol. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(98)00071-6