D-allo-threonine

• 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: D-allo-threonine
• 英文别名: (2R,3R)-2-acetamido-3-hydroxybutanoic acid
• 化学式: C₆H₁₁NO₄
• 分子量: 161.158
• InChiKey: PEDXUVCGOLSNLQ-NQXXGFSBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.9
• 重原子数：
  11
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  86.6
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  D-allo-threonine 在 四氮唑 、 palladium on activated charcoal 、 氢气 、 四丁基碘化铵 、 三乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 59.4h， 生成
  参考文献：
  名称：

  Switching Lysophosphatidylserine G Protein-Coupled Receptor Agonists to Antagonists by Acylation of the Hydrophilic Serine Amine

  摘要：

  DOI：

  10.1021/acs.jmedchem.1c00347
• 作为产物：
  描述：

  D-别苏氨酸 、 乙酸酐 在 溶剂黄146 作用下， 反应 24.5h， 生成 D-allo-threonine
  参考文献：
  名称：

  Switching Lysophosphatidylserine G Protein-Coupled Receptor Agonists to Antagonists by Acylation of the Hydrophilic Serine Amine

  摘要：

  DOI：

  10.1021/acs.jmedchem.1c00347

文献信息

• Peptides Constrained to Type VI β-Turns. 2. Antiparallel β-Ladder Formation
  作者：Kyonghee Kim、Juris P. Germanas

  DOI：10.1021/jo961181j

  日期：1997.5.1

  The preparation and characterization of an extensive series of bis-amino acid conjugates of a novel beta-turn mimic are described. The conjugates were prepared by coupling amino acid residues to the amino and carboxyl groups of the mimic, which represented the central two residues of a peptide constrained to the type VI turn conformation. The resultant adducts had the capability to form either singly or doubly hydrogen-bonded conformations, which represented beta-turn or antiparallel beta-ladder structures, respectively. In the majority of the bis-amino acid conjugates of the cis-lactam 1 (or its enantiomer), only the interior hydrogen bond, characteristic of the singly hydrogen-bonded conformation, was present, according to NMR and IR spectra. When the lactam 1 or its enantiomer were coupled to L-Phe at its carboxyl group and N-AcGly at its amino group, the spectral properties indicated the presence of the doubly hydrogen-bonded form. The results are consistent with other corkers' studies that demonstrated that aryl residues following Pro stabilize antiparallel type VI turn structures and that the propensity of an amino acid to adopt a beta-conformation in proteins is highly dependent on context.
• Switching Lysophosphatidylserine G Protein-Coupled Receptor Agonists to Antagonists by Acylation of the Hydrophilic Serine Amine
  作者：Misa Sayama、Akiharu Uwamizu、Masaya Ikubo、Luying Chen、Ge Yan、Yuko Otani、Asuka Inoue、Junken Aoki、Tomohiko Ohwada

  DOI：10.1021/acs.jmedchem.1c00347

  日期：2021.7.22