Boc-L-Tyr(OH)-D/L-Ala-OMe | 1278586-14-3

• 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: Boc-L-Tyr(OH)-D/L-Ala-OMe
• CAS: 1278586-14-3
• 化学式: C₁₈H₂₆N₂O₆
• 分子量: 366.414
• InChiKey: YLANGXTXNGHOMN-IAXJKZSUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.51
• 重原子数：
  26.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  113.96
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (4-3,4-3,5)12G2-CH2Cl 、 Boc-L-Tyr(OH)-D/L-Ala-OMe 在 potassium carbonate 作用下， 以 乙酸乙酯 为溶剂， 以40%的产率得到methyl ((S)-3-(4-((3,5-bis((3,4-bis((4-(dodecyloxy)benzyl)oxy)benzyl)oxy)benzyl)oxy)phenyl)-2-((tert-butoxycarbonyl)amino)propanoyl)alaninate
  参考文献：
  名称：

  Programming the Supramolecular Helical Polymerization of Dendritic Dipeptides via the Stereochemical Information of the Dipeptide

  摘要：

  Many natural biomacromolecules are homochiral and are built from constituents possessing identical handedness. The construction of synthetic molecules, macromolecules, and supramolecular structures with tailored stereochemical sequences can detail the relationship between chirality and function and provide insight into the process that leads to the selection of handedness and amplification of chirality. Dendritic dipeptides, previously reported from our laboratory, self-assemble into helical porous columns and serve as fundamental mimics of natural porous helix-forming proteins and supramolecular polymers. Herein, the synthesis of all stereochemical permutations of a self-assembling dendritic dipeptide including homochiral, heterochiral, and differentially racemized variants is reported. A combination of CD/UV-vis spectroscopy in solution and in film, X-ray diffraction, and differential scanning calorimetry studies in solid state established the role of the stereochemistry of the dipeptide on the thermodynamics and mechanism of self-assembly. It was found that the highest degree of stereochemical purity, enantiopure homochiral dendritic dipeptides, exhibits the most thermodynamically favorable self-assembly process in solution corresponding to the greatest degree of helical order and intracolumnar crystallization in solid state. Reducing the stereochemical purity of the dendritic dipeptide through heterochirality or by partially or fully racernizing the dendritic dipeptide destructively interferes with the self-assembly process. All dendritic dipeptides were shown to coassemble into single columns regardless of their stereochemistry. Because these columns exhibit no deracemization, the thermodynamic advantage of enantiopurity and homochirality suggests a mechanism for stereochemical selection and chiral amplification.

  DOI：

  10.1021/ja200280h
• 作为产物：
  描述：

  Boc-D-酪氨酸 、 DL-丙氨酸甲酯盐酸盐 在 N-甲基吗啉 、 2-氯-4,6-二甲氧基-1,3,5-三嗪 作用下， 以 乙酸乙酯 为溶剂， 以87%的产率得到Boc-L-Tyr(OH)-D/L-Ala-OMe
  参考文献：
  名称：

  Programming the Supramolecular Helical Polymerization of Dendritic Dipeptides via the Stereochemical Information of the Dipeptide

  摘要：

  Many natural biomacromolecules are homochiral and are built from constituents possessing identical handedness. The construction of synthetic molecules, macromolecules, and supramolecular structures with tailored stereochemical sequences can detail the relationship between chirality and function and provide insight into the process that leads to the selection of handedness and amplification of chirality. Dendritic dipeptides, previously reported from our laboratory, self-assemble into helical porous columns and serve as fundamental mimics of natural porous helix-forming proteins and supramolecular polymers. Herein, the synthesis of all stereochemical permutations of a self-assembling dendritic dipeptide including homochiral, heterochiral, and differentially racemized variants is reported. A combination of CD/UV-vis spectroscopy in solution and in film, X-ray diffraction, and differential scanning calorimetry studies in solid state established the role of the stereochemistry of the dipeptide on the thermodynamics and mechanism of self-assembly. It was found that the highest degree of stereochemical purity, enantiopure homochiral dendritic dipeptides, exhibits the most thermodynamically favorable self-assembly process in solution corresponding to the greatest degree of helical order and intracolumnar crystallization in solid state. Reducing the stereochemical purity of the dendritic dipeptide through heterochirality or by partially or fully racernizing the dendritic dipeptide destructively interferes with the self-assembly process. All dendritic dipeptides were shown to coassemble into single columns regardless of their stereochemistry. Because these columns exhibit no deracemization, the thermodynamic advantage of enantiopurity and homochirality suggests a mechanism for stereochemical selection and chiral amplification.

  DOI：

  10.1021/ja200280h