| 1449363-87-4

• 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
• CAS: 1449363-87-4
• 化学式: C₂₈H₄₅N₇O₈
• 分子量: 607.707
• InChiKey: XBUAFBIHXPLDLX-IZBJGVDFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.08
• 重原子数：
  43.0
• 可旋转键数：
  11.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  190.06
• 氢给体数：
  4.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  在 盐酸 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 1,4-二氧六环 、 甲醇 、 二氯甲烷 为溶剂， 反应 16.57h， 生成 ClNH₃-Ala-Pmh-DPro-Aib-DAla-DAla-OMe
  参考文献：
  名称：

  X-ray Crystal Structure of Teicoplanin A₂-2 Bound to a Catalytic Peptide Sequence via the Carrier Protein Strategy

  摘要：

  We report the X-ray crystal structure of a site-selective peptide catalyst moiety and teicoplanin A(2)-2 complex. The expressed protein ligation technique was used to couple T4 lysozyme (T4L) and a synthetic peptide catalyst responsible for the selective phosphorylation of the N-acetylglucosamine sugar in a teicoplanin A(2)-2 derivative. The T4L-Pmh-DPro-Aib-DAla-DAla construct was crystallized in the presence of teicoplanin A(2)-2. The resulting 2.3 angstrom resolution protein peptide teicoplanin complex crystal structure revealed that the nucleophilic nitrogen of N-methylimidazole in the Pmh residue is in closer proximity (7.6 angstrom) to the N-acetylglucosamine than the two other sugar rings present in teicoplanin (9.3 and 20.3 angstrom, respectively). This molecular arrangement is consistent with the observed selectivity afforded by the peptide-based catalyst when it is applied to a site-selective phosphorylation reaction involving a teicoplanin A(2)-2 derivative.

  DOI：

  10.1021/jo501625f
• 作为产物：
  描述：

  N-Boc-D-alanyl-D-alanine methyl ester 在 盐酸 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 为溶剂， 反应 43.15h， 生成
  参考文献：
  名称：

  Asymmetric Catalysis at a Distance: Catalytic, Site-Selective Phosphorylation of Teicoplanin

  摘要：

  We report three distinct, peptide-based catalysts that enable site-selective phosphorylation of three distinct hydroxyl groups within the complex glycopeptide antibiotic teicoplanin A(2)-2. Two of the catalysts are based on a design that capitalizes on a catalyst substrate interaction that mimics the biological mechanism of action for teicoplanin. These catalysts are based on a DXaa-DXaa peptide motif that is known to target the teicoplanin structure in a specific manner. The third was identified through evaluation of a set of catalysts that had been developed for historically distinct projects. Each catalyst contains additional functionality designed to dispose a catalytic moiety (a nudeophilic alkylimidazole) at a different region of the glycopeptide structure. A combination of mass spectrometry and 2D-NMR spectroscopy allowed structural assignment of the distinct phosphorylated teicoplanin derivatives. Mechanistic studies are also reported that support the hypotheses that led to the discovery of the catalysts. In this manner, small molecule catalysts have been achieved that allow rational, catalytic control over reactions at sites that are separated by 11.6, 16.5, and nearly 17.7 angstrom, based on the X-ray crystal structure of teicoplanin A(2)-2. Finally, we report the biological activity of the new phosphorylated teicoplanin analogs and compare the results to the natural product itself.

  DOI：

  10.1021/ja406067v