4-isopropyl-2-phenylpyrimidine-5-carbonitrile | 1228383-81-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: 4-isopropyl-2-phenylpyrimidine-5-carbonitrile
• 英文别名: 2-Phenyl-4-propan-2-ylpyrimidine-5-carbonitrile
• CAS: 1228383-81-0
• 化学式: C₁₄H₁₃N₃
• 分子量: 223.277
• InChiKey: IOOAEKFBXBFDRG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  17
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  49.6
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  2-isobutyryl-3-dimethylaminoacrylonitrile 、 苄脒盐酸盐 在 sodium ethanolate 作用下， 以 乙醇 为溶剂， 反应 0.67h， 以87%的产率得到4-isopropyl-2-phenylpyrimidine-5-carbonitrile
  参考文献：
  名称：

  Facile Iterative Synthesis of 2,5-Terpyrimidinylenes as Nonpeptidic α-Helical Mimics

  摘要：

  A facile iterative synthesis of 2,5-terpyrimidinylenes that are structurally analogous to alpha-helix mimics is presented. Condensation of amidines with readily prepared alpha,beta-unsaturated alpha-cyanoketones gives 5-cyano-substituted pyrimidines. Iterative transformation of the 5-cyano group into an amidine allows synthesis of 2,5-terpyrimidinylenes with variable groups at the 4-, 4'-, and 4 ''-positions. These compounds are designed to mimic the i, i + 4, and i + 7 sites of an alpha-helix.

  DOI：

  10.1021/jo100272d

文献信息

• [EN] ALPHA-HELIX MIMETIC USING A 2,5-OLIGOPYRIMIDINE SCAFFOLD<br/>[FR] STRUCTURE MIMÉTIQUE D'HÉLICE ALPHA UTILISANT UN SQUELETTE 2,5-OLIGOPYRIMIDINE
  申请人：UNIV SOUTH FLORIDA

  公开号：WO2010083501A2

  公开（公告）日：2010-07-22

  Alpha-helix mimetics and associated methods of making are provided. These compounds are constructed using a 2,5-oligopyrimidine scaffold. The semi-rigid scaffold holds individual side chain-like residues in orientations that mimic the orientations of side chain residues of an ?-helical protein domain. The new scaffold is easier to make than previous scaffolds and has much more favorable physical properties than previous alpha-helix mimics. The amphiphilic alpha-helix mimetics have application for making libraries and for treating diseases or conditions effected by the inhibition or disruption of interactions with the alpha helix of a protein.