(R)-valic acid 2-naphthacyl ester | 1361944-75-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: (R)-valic acid 2-naphthacyl ester
• 英文别名: (2-naphthalen-2-yl-2-oxoethyl) (2R)-2-hydroxy-3-methylbutanoate
• CAS: 1361944-75-3
• 化学式: C₁₇H₁₈O₄
• 分子量: 286.328
• InChiKey: YAECODBDEDDZSA-MRXNPFEDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  21
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  63.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  D-缬氨酸 在 硫酸 、 水 、 三乙胺 、 sodium nitrite 作用下， 以 乙酸乙酯 为溶剂， 反应 13.0h， 生成 (R)-valic acid 2-naphthacyl ester
  参考文献：
  名称：

  Symplocin A, a Linear Peptide from the Bahamian CyanobacteriumSymplocasp. Configurational Analysis ofN,N-Dimethylamino Acids by Chiral-Phase HPLC of Naphthacyl Esters

  摘要：

  The absolute stereostructures of the components of symplocin A (3), a new N,N-dimethyl-terminated peptide from the Bahamian cyanobacterium Symploca sp., were assigned from spectroscopic analysis, including MS, 2D NMR, and Marfey's analysis. The complete absolute configuration of symplocin A, including the unexpected D-configurations of the terminal N,N-dimethylisoleucine and valic acid residues, was assigned by chiral-phase HPLC of the corresponding 2-naphthacyl esters, a highly sensitive, complementary strategy for assignment of N-blocked peptide residues where Marfey's method is ineffectual or other methods fall short. Symplocin A exhibited potent activity as an inhibitor of cathepsin E (IC50 300 pM).

  DOI：

  10.1021/np200861n

文献信息

• Symplocin A, a Linear Peptide from the Bahamian Cyanobacterium<i>Symploca</i>sp. Configurational Analysis of<i>N</i>,<i>N</i>-Dimethylamino Acids by Chiral-Phase HPLC of Naphthacyl Esters
  作者：Tadeusz F. Molinski、Kirk A. Reynolds、Brandon I. Morinaka

  DOI：10.1021/np200861n

  日期：2012.3.23

  The absolute stereostructures of the components of symplocin A (3), a new N,N-dimethyl-terminated peptide from the Bahamian cyanobacterium Symploca sp., were assigned from spectroscopic analysis, including MS, 2D NMR, and Marfey's analysis. The complete absolute configuration of symplocin A, including the unexpected D-configurations of the terminal N,N-dimethylisoleucine and valic acid residues, was assigned by chiral-phase HPLC of the corresponding 2-naphthacyl esters, a highly sensitive, complementary strategy for assignment of N-blocked peptide residues where Marfey's method is ineffectual or other methods fall short. Symplocin A exhibited potent activity as an inhibitor of cathepsin E (IC50 300 pM).