tert-butyl 2-(2-(2-(2-(methoxycarbonyl)phenylcarbamoyl)pyrrolidine-1-carbonyl)phenylcarbamoyl)pyrrolidine-1-carboxylate | 1094297-15-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: tert-butyl 2-(2-(2-(2-(methoxycarbonyl)phenylcarbamoyl)pyrrolidine-1-carbonyl)phenylcarbamoyl)pyrrolidine-1-carboxylate
• CAS: 1094297-15-0
• 化学式: C₃₀H₃₆N₄O₇
• 分子量: 564.638
• InChiKey: PPWIZQUZZZFLOU-ZEQRLZLVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.05
• 重原子数：
  41.0
• 可旋转键数：
  6.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  134.35
• 氢给体数：
  2.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  tert-butyl 2-(2-(2-(2-(methoxycarbonyl)phenylcarbamoyl)pyrrolidine-1-carbonyl)phenylcarbamoyl)pyrrolidine-1-carboxylate 在 lithium hydroxide 、 水 作用下， 以 甲醇 为溶剂， 反应 12.0h， 生成 2-(1-(2-(1-(tert-butylcarbonyl)pyrrolidine-2-carboxamido)-benzoyl)pyrrolidine-2-carboxamido)benzoic acid
  参考文献：
  名称：

  Sequence-Specific Unusual (1→2)-Type Helical Turns in α/β-Hybrid Peptides

  摘要：

  This article describes novel conformationally ordered (alpha/beta-hybrid peptides consisting of repeating L-proline-anthranilic acid building blocks. These oligomers adopt a compact, right-handed helical architecture determined by the intrinsic conformational preferences of the individual amino acid residues. The striking feature of these oligomers is their ability to display an unusual periodic pseudo beta-turn network of nine-membered hydrogen-bonded rings formed in the forward direction of the sequence by 1-->2 amino acid interactions both in solid-state and in solution. Conformational investigations of several of these oligomers by single-crystal X-ray diffraction, solution-state NMR, and ab initio MO theory suggest that the characteristic steric and dihedral angle restraints exerted by proline are essential for stabilizing the unusual pseudo beta-turn network found in these oligomers. Replacing proline by the conformationally flexible analogue alanine (Ala) or by the conformationally more constrained alpha-amino isobutyric acid (Aib) had an adverse effect on the stabilization of this structural architecture. These findings increase the potential to design novel secondary structure elements profiting from the steric and dihedral angle constraints of the amino acid constituents and help to augment the conformational space available for synthetic oligomer design with diverse backbone structures.

  DOI：

  10.1021/ja804297f
• 作为产物：
  描述：

  methyl 2-(pyrrolidine-2-carboxamido)benzoate hydrochloride 、 2-(1-(tert-butoxycarbonyl)pyrrolidine-2-carboxamido)benzoic acid 在 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 N,N-二异丙基乙胺 作用下， 反应 12.0h， 以78%的产率得到tert-butyl 2-(2-(2-(2-(methoxycarbonyl)phenylcarbamoyl)pyrrolidine-1-carbonyl)phenylcarbamoyl)pyrrolidine-1-carboxylate
  参考文献：
  名称：

  Sequence-Specific Unusual (1→2)-Type Helical Turns in α/β-Hybrid Peptides

  摘要：

  This article describes novel conformationally ordered (alpha/beta-hybrid peptides consisting of repeating L-proline-anthranilic acid building blocks. These oligomers adopt a compact, right-handed helical architecture determined by the intrinsic conformational preferences of the individual amino acid residues. The striking feature of these oligomers is their ability to display an unusual periodic pseudo beta-turn network of nine-membered hydrogen-bonded rings formed in the forward direction of the sequence by 1-->2 amino acid interactions both in solid-state and in solution. Conformational investigations of several of these oligomers by single-crystal X-ray diffraction, solution-state NMR, and ab initio MO theory suggest that the characteristic steric and dihedral angle restraints exerted by proline are essential for stabilizing the unusual pseudo beta-turn network found in these oligomers. Replacing proline by the conformationally flexible analogue alanine (Ala) or by the conformationally more constrained alpha-amino isobutyric acid (Aib) had an adverse effect on the stabilization of this structural architecture. These findings increase the potential to design novel secondary structure elements profiting from the steric and dihedral angle constraints of the amino acid constituents and help to augment the conformational space available for synthetic oligomer design with diverse backbone structures.

  DOI：

  10.1021/ja804297f