杜 欣 张书恩 刘军政 聂菲璘 叶 菲 田金英 肖志艳. 丙二酸类PTP1B抑制剂的设计、合成及活性研究J. 药学学报, 2012,47(3): 367-373.
引用本文: 杜 欣 张书恩 刘军政 聂菲璘 叶 菲 田金英 肖志艳. 丙二酸类PTP1B抑制剂的设计、合成及活性研究J. 药学学报, 2012,47(3): 367-373.
shu
DU Xin, Zhang Shu-En, Liu Jun-Zheng, Nie Fei-Lin, Xie Fei, Tian Jin-Yang, Xiao Zhi-Yan. Design, synthesis and evaluation of malonic acid-based PTP1B inhibitorsJ. 药学学报, 2012,47(3): 367-373.
Citation: DU Xin, Zhang Shu-En, Liu Jun-Zheng, Nie Fei-Lin, Xie Fei, Tian Jin-Yang, Xiao Zhi-Yan. Design, synthesis and evaluation of malonic acid-based PTP1B inhibitorsJ. 药学学报, 2012,47(3): 367-373.
shu

丙二酸类PTP1B抑制剂的设计、合成及活性研究

Design, synthesis and evaluation of malonic acid-based PTP1B inhibitors

    摘要
  • 摘要:

    蛋白酪氨酸磷酸酶 (protein tyrosine phosphatase, PTP) 1B是治疗2型糖尿病 (T2DM) 及肥胖症的潜在靶点。磷酸酪氨酸 (pTyr) 是PTP1B去磷酸化作用的底物, 本文以丙二酸基团模拟pTyr分子中的磷酸酯, 设计合成了丙二酸类PTP1B抑制剂1～7。抑酶活性评价显示, 化合物3和4对人重组PTP1B的半数抑制浓度IC50分别为7.66和1.88 μmol·L−1。

     

    Abstract:

    Protein tyrosine phosphatase (PTP) 1B is a potential target for the treatment of diabetes and obesity.  Phosphotyrosine (pTyr) is the substrate for PTP1B dephosphorylation.  Malonic acid moiety was used herein as a mimic of the phosphate group in pTyr, and novel malonic acid derivatives 1−7 were designed, synthesized and evaluated as PTP1B inhibitors.  Results from enzymatic assays indicated that compounds 3 and 4 exhibited potent inhibition against human recombinant PTP1B with IC50 values of 7.66 and 1.88 μmol·L−1, respectively.

     

    • HTML全文
    • 参考文献(0)
    • 相关文章
    • 施引文献
  • 资源附件(0)

/

返回文章
返回