| 1235447-10-5

• 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: 1235447-10-5
• 化学式: C₁₀H₁₃N₃O₂
• 分子量: 207.232
• InChiKey: ZIDUNKJQJQJGLR-QMMMGPOBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.62
• 重原子数：
  15.0
• 可旋转键数：
  2.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  55.32
• 氢给体数：
  0.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  五氟苯 、 在 2,2'-硫代二丙烷 、 palladium diacetate 、 silver carbonate 作用下， 以 1,4-二氧六环 为溶剂， 以78 %的产率得到methyl (5-(perfluorophenyl)pyrimidin-2-yl)prolinate
  参考文献：
  名称：

  Substrate-controlled divergent remote C–H and N–H polyfluoroarylation of 2-aminopyrimidines with polyfluoroarenes via Pd(ii)/Pd(0) catalysis

  摘要：

  Substrate-controlled product divergence is demonstrated in Pd-catalyzed reaction of 2-aminopyrimidines. Remote C5–H polyfluoroarylation occurs with N-alkylpyrimidine-2-amines, while N–H polyfluoroarylation is dominant for N-aryl-pyrimidine-2-amines.

  DOI：

  10.1039/d4cc01518e
• 作为产物：
  描述：

  L-脯氨酸 在 氯化亚砜 、 三乙胺 作用下， 以 乙醇 为溶剂， 生成
  参考文献：
  名称：

  Substrate-controlled divergent remote C–H and N–H polyfluoroarylation of 2-aminopyrimidines with polyfluoroarenes via Pd(ii)/Pd(0) catalysis

  摘要：

  Substrate-controlled product divergence is demonstrated in Pd-catalyzed reaction of 2-aminopyrimidines. Remote C5–H polyfluoroarylation occurs with N-alkylpyrimidine-2-amines, while N–H polyfluoroarylation is dominant for N-aryl-pyrimidine-2-amines.

  DOI：

  10.1039/d4cc01518e

文献信息

• Basic techniques of working on a solid phase: From ABC of the peptide synthesis to libraries of non-natural amino acids
  作者：E. V. Babaev、D. S. Ermolat’ev

  DOI：10.1134/s107036321012025x

  日期：2010.12

  Libraries of hardly available amino acids bearing a heteroaromatic ring (2-pyrimidyl, substituted 2-pyridyl or 2-thiazolyl) at the amino group were prepared using solid-phase synthesis on various resins. The synthesized compounds are structurally similar to some known antidiabetic drugs. The paper combines features of a review (elementary introduction to the solid-phase synthesis methodology and technique for beginners and selected methods from peptide chemistry) and step-by-step experimental protocols (tested by the authors) useful as a methodic tool. The presented protocols (immobilization and modification of amino acids, placing and removal of common protective groups) require no sophisticated equipment and may be useful as pictorial introductory tasks for students education.