(3S,9S,12S,13S)-12-azido-9-benzyl-3-isobutyl-13-methyl-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetraone | 1378482-62-2

• 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: (3S,9S,12S,13S)-12-azido-9-benzyl-3-isobutyl-13-methyl-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetraone
• 英文别名: cyclo[Gly-Leu-bAla(2R-N3,3S-Me)-Phe]；(3S,9S,12R,13S)-12-azido-9-benzyl-13-methyl-3-(2-methylpropyl)-1,4,7,10-tetrazacyclotridecane-2,5,8,11-tetrone
• CAS: 1378482-62-2
• 化学式: C₂₁H₂₉N₇O₄
• 分子量: 443.506
• InChiKey: MJHVDICJAOAGBA-OWIUFQIYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.6
• 重原子数：
  32
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  131
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  N-烯丙氧羰基-L-亮氨酸 在 四(三苯基膦)钯 、 巴比妥酸 、 sodium azide 、 N-羟基-7-氮杂苯并三氮唑 、 PyBOP 、 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 作用下， 以 二氯甲烷 、 氯仿 、 二甲基亚砜 、 N,N-二甲基甲酰胺 为溶剂， 反应 39.0h， 生成 (3S,9S,12S,13S)-12-azido-9-benzyl-3-isobutyl-13-methyl-1,4,7,10-tetraazacyclotridecane-2,5,8,11-tetraone
  参考文献：
  名称：

  A Versatile Scaffold for Site-Specific Modification of Cyclic Tetrapeptides

  摘要：

  A novel scaffold that can be used to prepare conformationally homogeneous cyclic tetrapeptides equipped with a beta-amino acid residue is disclosed. It Is shown that regioselective structural modification can be accomplished using thiols and azide nucleophiles, commonly associated with rich downstream chemistry. The method should find application in efforts to constrain privileged tripeptide sequences in rigid molecular scaffolds.

  DOI：

  10.1021/ol301178r

文献信息

• A Versatile Scaffold for Site-Specific Modification of Cyclic Tetrapeptides
  作者：Christopher J. White、Andrei K. Yudin

  DOI：10.1021/ol301178r

  日期：2012.6.1

  A novel scaffold that can be used to prepare conformationally homogeneous cyclic tetrapeptides equipped with a beta-amino acid residue is disclosed. It Is shown that regioselective structural modification can be accomplished using thiols and azide nucleophiles, commonly associated with rich downstream chemistry. The method should find application in efforts to constrain privileged tripeptide sequences in rigid molecular scaffolds.