[(S)-1-((S)-2-Carbamoyl-pyrrolidine-1-carbonyl)-4-(2-ethoxy-3,4-dioxo-cyclobut-1-enylamino)-butyl]-carbamic acid 9H-fluoren-9-ylmethyl ester | 861996-32-9

• 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: [(S)-1-((S)-2-Carbamoyl-pyrrolidine-1-carbonyl)-4-(2-ethoxy-3,4-dioxo-cyclobut-1-enylamino)-butyl]-carbamic acid 9H-fluoren-9-ylmethyl ester
• CAS: 861996-32-9
• 化学式: C₃₁H₃₄N₄O₇
• 分子量: 574.634
• InChiKey: HYXHNTKXVFCVHU-ZEQRLZLVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.26
• 重原子数：
  42.0
• 可旋转键数：
  12.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  157.13
• 氢给体数：
  3.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  [(S)-1-((S)-2-Carbamoyl-pyrrolidine-1-carbonyl)-4-(2-ethoxy-3,4-dioxo-cyclobut-1-enylamino)-butyl]-carbamic acid 9H-fluoren-9-ylmethyl ester 在 盐酸 作用下， 以 四氢呋喃 为溶剂， 反应 20.0h， 生成 [(S)-1-((S)-2-Carbamoyl-pyrrolidine-1-carbonyl)-4-(2-hydroxy-3,4-dioxo-cyclobut-1-enylamino)-butyl]-carbamic acid 9H-fluoren-9-ylmethyl ester
  参考文献：
  名称：

  Control of Protein−Protein Interactions:  Structure-Based Discovery of Low Molecular Weight Inhibitors of the Interactions between Pin1 WW Domain and Phosphopeptides

  摘要：

  Interactions involving phosphorylated Ser/Thr-Pro motifs in proteins play a key role in numerous regulatory processes in the cell. Here, we investigate potential ligands of the WW binding domain of Pin1 in order to inhibit protein-protein interactions between Pin1 and phosphopeptides. Our structure-based strategy implies the synthesis of analogues of the Ac-Thr(PO3H2)-Pro-NH2 dipeptide and relies on high resolution NMR spectroscopy to accurately measure the affinity constants even in the high micromolar range.

  DOI：

  10.1021/jm0500119
• 作为产物：
  描述：

  [(S)-5-((S)-2-Carbamoyl-pyrrolidin-1-yl)-4-(9H-fluoren-9-ylmethoxycarbonylamino)-5-oxo-pentyl]-carbamic acid tert-butyl ester 在 盐酸 、 三乙胺 作用下， 以 1,4-二氧六环 、 乙醇 、 二氯甲烷 为溶剂， 反应 15.0h， 生成 [(S)-1-((S)-2-Carbamoyl-pyrrolidine-1-carbonyl)-4-(2-ethoxy-3,4-dioxo-cyclobut-1-enylamino)-butyl]-carbamic acid 9H-fluoren-9-ylmethyl ester
  参考文献：
  名称：

  Control of Protein−Protein Interactions:  Structure-Based Discovery of Low Molecular Weight Inhibitors of the Interactions between Pin1 WW Domain and Phosphopeptides

  摘要：

  Interactions involving phosphorylated Ser/Thr-Pro motifs in proteins play a key role in numerous regulatory processes in the cell. Here, we investigate potential ligands of the WW binding domain of Pin1 in order to inhibit protein-protein interactions between Pin1 and phosphopeptides. Our structure-based strategy implies the synthesis of analogues of the Ac-Thr(PO3H2)-Pro-NH2 dipeptide and relies on high resolution NMR spectroscopy to accurately measure the affinity constants even in the high micromolar range.

  DOI：

  10.1021/jm0500119