cis-2-(9-Fluorenylmethoxycarbonylamino)cyclohex-3-enecarboxylic acid | 1279129-64-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: cis-2-(9-Fluorenylmethoxycarbonylamino)cyclohex-3-enecarboxylic acid
• 英文别名: (1R,2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)cyclohex-3-ene-1-carboxylic acid
• CAS: 1279129-64-4
• 化学式: C₂₂H₂₁NO₄
• 分子量: 363.413
• InChiKey: OTYJADWWVDSUOQ-QUCCMNQESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  27
• 可旋转键数：
  5
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  75.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  cis-2-(9-Fluorenylmethoxycarbonylamino)cyclohex-3-enecarboxylic acid 、 rac,cis-2-(9-fluorenylmethoxycarbonylamino)-cyclohex-3-ene carboxylic acid 在 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 、 三氟乙酸 作用下， 以 水 为溶剂， 反应 3.0h， 以48%的产率得到
  参考文献：
  名称：

  Building β-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly

  摘要：

  The ability of the beta-peptidic H10/12 helix to tolerate side-chains containing six-membered alicyclic rings was studied. cis-2-Aminocyclohex-3-ene carboxylic acid (cis-ACHEC) res dues afforded H10/12 helix formation with alternating backbone configuration. Conformational polymorphism was observed for the alternating cis-ACHC hexamer, where chemical exchange takes place between the major left-handed H10/12 helix and a minor folded conformation. The hydrophobically driven self-assembly was achieved for the cis-ACHC-containing helix which was observed as vesicles similar to 100 nm in diameter.

  DOI：

  10.1021/ol102494m

文献信息

• Building β-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly
  作者：István M. Mándity、Livia Fülöp、Elemér Vass、Gábor K. Tóth、Tamás A. Martinek、Ferenc Fülöp

  DOI：10.1021/ol102494m

  日期：2010.12.3

  The ability of the beta-peptidic H10/12 helix to tolerate side-chains containing six-membered alicyclic rings was studied. cis-2-Aminocyclohex-3-ene carboxylic acid (cis-ACHEC) res dues afforded H10/12 helix formation with alternating backbone configuration. Conformational polymorphism was observed for the alternating cis-ACHC hexamer, where chemical exchange takes place between the major left-handed H10/12 helix and a minor folded conformation. The hydrophobically driven self-assembly was achieved for the cis-ACHC-containing helix which was observed as vesicles similar to 100 nm in diameter.