cyclo[-Arg(NO2)-Lys(Z)-Asp(OBn)-Val-Tyr-Arg(NO2)-Lys(Z)-Asp(OBn)-Val-Tyr]

• 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: cyclo[-Arg(NO2)-Lys(Z)-Asp(OBn)-Val-Tyr-Arg(NO2)-Lys(Z)-Asp(OBn)-Val-Tyr]
• 英文别名: cyclo[Arg(NO2)(NO2)-Lys(Cbz)(Cbz)-Asp(OBn)(OBn)-Val-Tyr-Arg(NO2)(NO2)-Lys(Cbz)(Cbz)-Asp(OBn)(OBn)-Val-Tyr]；benzyl 2-[(2S,5S,8S,11S,14S,17S,20S,23S,26S,29S)-8,23-bis[(4-hydroxyphenyl)methyl]-11,26-bis[3-[(N-nitrocarbamimidoyl)amino]propyl]-3,6,9,12,15,18,21,24,27,30-decaoxo-17-(2-oxo-2-phenylmethoxyethyl)-14,29-bis[4-(phenylmethoxycarbonylamino)butyl]-5,20-di(propan-2-yl)-1,4,7,10,13,16,19,22,25,28-decazacyclotriacont-2-yl]acetate
• 化学式: C₉₀H₁₁₆N₂₀O₂₄
• 分子量: 1862.03
• InChiKey: AJVPLTSGRKBWFA-WFCNBSCFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.1
• 重原子数：
  134
• 可旋转键数：
  44
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  648
• 氢给体数：
  20
• 氢受体数：
  26

反应信息

• 作为产物：
  描述：

  H-Arg(NO2)-Lys(Z)-Asp(OBn)-Val-Tyr-OH 在 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 1.0h， 以2%的产率得到cyclo[-Arg(NO2)-Lys(Z)-Asp(OBn)-Val-Tyr-Arg(NO2)-Lys(Z)-Asp(OBn)-Val-Tyr]
  参考文献：
  名称：

  Cyclization of all-l-Pentapeptides by Means of 1-Hydroxy-7-azabenzotriazole-Derived Uronium and Phosphonium Reagents

  摘要：

  Due to their restricted conformational flexibility, cyclic peptides are of great interest in connection with structure-activity relationships, especially the elucidation of bioactive conformations. For linear peptides that do not contain turn structure-inducing amino acid residues, the cyclization reaction may be an inherently improbable or slow process, and side reactions, such as cyclodimerization and epimerization at the C-terminal residue, may dominate. A number of 1-hydroxy-7-azabenzotriazole-based onium salts were examined for cyclization of thymopentin-derived pentapeptides and the results compared with data from more conventional coupling reagents. The azabenzotriazol-derived coupling reagents stood out as being the most effective by far. The cyclizations proceed extremely rapidly, and in contrast to other coupling reagents, C-terminal epimerization was generally less than 10%. C-terminal D-amino acid residues favor the formation of monocyclic pentapeptide rings. A similar effect was observed for cyclization of linear N-methylamino acid-containing peptides, suggesting that reversible amide bond alkylation such as Hmb-modification should be useful in promoting the cyclization of pepitdes devoid of turn-inducing amino acid residues.

  DOI：

  10.1021/jo951108d

文献信息

• Cyclization of <i>all</i>-<scp>l</scp>-Pentapeptides by Means of 1-Hydroxy-7-azabenzotriazole-Derived Uronium and Phosphonium Reagents
  作者：Angelika Ehrlich、Hans-Ulrich Heyne、Rüdiger Winter、Michael Beyermann、Hanka Haber、Louis A. Carpino、Michael Bienert

  DOI：10.1021/jo951108d

  日期：1996.1.1

  Due to their restricted conformational flexibility, cyclic peptides are of great interest in connection with structure-activity relationships, especially the elucidation of bioactive conformations. For linear peptides that do not contain turn structure-inducing amino acid residues, the cyclization reaction may be an inherently improbable or slow process, and side reactions, such as cyclodimerization and epimerization at the C-terminal residue, may dominate. A number of 1-hydroxy-7-azabenzotriazole-based onium salts were examined for cyclization of thymopentin-derived pentapeptides and the results compared with data from more conventional coupling reagents. The azabenzotriazol-derived coupling reagents stood out as being the most effective by far. The cyclizations proceed extremely rapidly, and in contrast to other coupling reagents, C-terminal epimerization was generally less than 10%. C-terminal D-amino acid residues favor the formation of monocyclic pentapeptide rings. A similar effect was observed for cyclization of linear N-methylamino acid-containing peptides, suggesting that reversible amide bond alkylation such as Hmb-modification should be useful in promoting the cyclization of pepitdes devoid of turn-inducing amino acid residues.