(2S)-1-[(2S)-2-amino-3-[4-(1-methyltriazol-4-yl)phenyl]propanoyl]pyrrolidine-2-carbonitrile;hydrochloride | 1429503-27-4

• 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
• 英文名称: (2S)-1-[(2S)-2-amino-3-[4-(1-methyltriazol-4-yl)phenyl]propanoyl]pyrrolidine-2-carbonitrile;hydrochloride
• CAS: 1429503-27-4
• 化学式: C₁₇H₂₀N₆O*ClH
• 分子量: 360.846
• InChiKey: PTOZBZBTZAOHNA-YYLIZZNMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.29
• 重原子数：
  25
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.41
• 拓扑面积：
  101
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  在 盐酸 、 copper(ll) sulfate pentahydrate 、 sodium ascorbate 作用下， 以 乙醚 、 乙醇 、 二氯甲烷 为溶剂， 生成 (2S)-1-[(2S)-2-amino-3-[4-(1-methyltriazol-4-yl)phenyl]propanoyl]pyrrolidine-2-carbonitrile;hydrochloride
  参考文献：
  名称：

  Design, Synthesis, Biological Evaluation, and Docking Studies of (S)-Phenylalanine Derivatives with a 2-Cyanopyrrolidine Moiety as Potent Dipeptidyl Peptidase 4 Inhibitors

  摘要：

  A novel series of (S)‐phenylalanine derivatives with a 2‐cyanopyrrolidine moiety were designed and synthesized through a rational drug design strategy. Biological evaluation revealed that most tested compounds were potent dipeptidyl peptidase 4 (DPP‐4) inhibitors; among them, the cyclopropyl‐substituted phenylalanine derivative 11h displayed the most potent DPP‐4 inhibitory activity with an IC50 value of 0.247 μm. In addition, molecular docking analysis of the representative compounds 11h, 11k, and 15a were performed, which not only revealed the impact of binding modes on DPP‐4 inhibitory activity but also provided additional methodological values for design and optimization.

  DOI：

  10.1111/cbdd.12139

文献信息

• Design, Synthesis, Biological Evaluation, and Docking Studies of (<i>S</i>)-Phenylalanine Derivatives with a 2-Cyanopyrrolidine Moiety as Potent Dipeptidyl Peptidase 4 Inhibitors
  作者：Yang Liu、Yizhe Wu、Haoshu Wu、Li Tang、Peng Wu、Tao Liu、Yongzhou Hu

  DOI：10.1111/cbdd.12139

  日期：2013.8

  A novel series of (S)‐phenylalanine derivatives with a 2‐cyanopyrrolidine moiety were designed and synthesized through a rational drug design strategy. Biological evaluation revealed that most tested compounds were potent dipeptidyl peptidase 4 (DPP‐4) inhibitors; among them, the cyclopropyl‐substituted phenylalanine derivative 11h displayed the most potent DPP‐4 inhibitory activity with an IC50 value of 0.247 μm. In addition, molecular docking analysis of the representative compounds 11h, 11k, and 15a were performed, which not only revealed the impact of binding modes on DPP‐4 inhibitory activity but also provided additional methodological values for design and optimization.