| 500800-65-7

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• CAS: 500800-65-7
• 化学式: C₁₉H₃₀N₂O₅
• 分子量: 366.458
• InChiKey: NUCNMLCNBFWKIW-CVEARBPZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.29
• 重原子数：
  26.0
• 可旋转键数：
  9.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  99.88
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  在 1-羟基苯并三唑 、 1-[3-(dimethylamino)-propyl]-3-ethylcarbodiimide methiodide 、 三乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 5.0h， 生成
  参考文献：
  名称：

  A Reverse Turn Structure Induced by a d,l-α-Aminoxy Acid Dimer

  摘要：

  Our previous work revealed that two adjacent D-a-aminoxy acids could form two homochiral N-O turns, with the backbone folding into an extended helical structure (1.8(8)-helix). Here, we report the conformational studies of linear peptides 3-6, which contain a D,L-alpha-aminoxy acid dimer segment. The NMR and X-ray analysis of 3 showed that it folded into a loop conformation with two heterochiral N-O turns. This loop segment can be used to constrain tetrapeptides 4 and 6 to form a reverse turn structure. H-1 NMR dilution studies, DMSO-d(6) addition studies, and 2D-NOESY data indicated that tetrapeptides 4 and 6 folded into reverse turn conformations featured by a head-to-tail 16-membered-ring intramolecular hydrogen bond. In contrast, tetrapeptide 5 with L-Ala instead of Gly or D-Ala as the N-terminal amino acid could not form the desired reverse turn structure for steric reasons. Quantum mechanics calculations showed that model pentamide 7, with the same substitution pattern of 4, adopted a novel reverse turn conformation featuring two heterochiral N-O turns (each of an 8-membered ring hydrogen bond), a cross-strand 16-membered ring hydrogen bond, and a 7-membered ring gamma-turn.

  DOI：

  10.1021/ja029514j
• 作为产物：
  描述：

  (2R)-2-[(1,3-二氢-1,3-二氧代-2H-异吲哚-2-基)氧基]-4-甲基-戊酸 在 1-羟基苯并三唑 、 一水合肼 、 1-[3-(dimethylamino)-propyl]-3-ethylcarbodiimide methiodide 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 2.5h， 生成
  参考文献：
  名称：

  A Reverse Turn Structure Induced by a d,l-α-Aminoxy Acid Dimer

  摘要：

  Our previous work revealed that two adjacent D-a-aminoxy acids could form two homochiral N-O turns, with the backbone folding into an extended helical structure (1.8(8)-helix). Here, we report the conformational studies of linear peptides 3-6, which contain a D,L-alpha-aminoxy acid dimer segment. The NMR and X-ray analysis of 3 showed that it folded into a loop conformation with two heterochiral N-O turns. This loop segment can be used to constrain tetrapeptides 4 and 6 to form a reverse turn structure. H-1 NMR dilution studies, DMSO-d(6) addition studies, and 2D-NOESY data indicated that tetrapeptides 4 and 6 folded into reverse turn conformations featured by a head-to-tail 16-membered-ring intramolecular hydrogen bond. In contrast, tetrapeptide 5 with L-Ala instead of Gly or D-Ala as the N-terminal amino acid could not form the desired reverse turn structure for steric reasons. Quantum mechanics calculations showed that model pentamide 7, with the same substitution pattern of 4, adopted a novel reverse turn conformation featuring two heterochiral N-O turns (each of an 8-membered ring hydrogen bond), a cross-strand 16-membered ring hydrogen bond, and a 7-membered ring gamma-turn.

  DOI：

  10.1021/ja029514j

文献信息

• Cyclic Hexapeptide of <scp>d</scp>,<scp>l</scp>-α-Aminoxy Acids as a Selective Receptor for Chloride Ion
  作者：Dan Yang、Jin Qu、Wei Li、Yu-Hui Zhang、Yi Ren、De-Ping Wang、Yun-Dong Wu

  DOI：10.1021/ja027073y

  日期：2002.10.1

  from linear hexapeptide 1 of alternating d- and l-α-aminoxy acids, was found to adopt a C3 symmetric and bracelet-like conformation with consecutive eight-membered-ring hydrogen bonds (N−O turns) in nonpolar solvents, similar to that of valinomycin, a cyclodepsipeptide that binds cations selectively. However, 2 showed affinities for halide ions with selectivity following the order of Cl- ≫ F- ≫ Br-

  由交替 d- 和 l-α-氨基酸的线性六肽 1 制备的环状六肽 2 被发现采用 C3 对称和手镯状构象，在非极性中具有连续的八元环氢键（N-O 转角）溶剂，类似于缬氨霉素，一种选择性结合阳离子的环缩肽。然而，2 显示出对卤离子的亲和力，其选择性遵循 Cl- ≫ F- ≫ Br- 的顺序。在 CD2Cl2 中观察到的 Cl- (Ka = 11880 M-1) 选择性高于 F- (Ka = 30 M-1) 表明 2 对卤离子的选择性主要受尺寸互补性而不是氢键控制力量。在 Cl- 离子结合后，2 的原始手镯状构象变成了相当平坦的构象，所有六个酰胺 NH 都指向内部，与 Cl- 形成氢键。