Chinese Journal of Organic Chemistry ›› 2019, Vol. 39 ›› Issue (12): 3446-3453.DOI: 10.6023/cjoc201908022 Previous Articles     Next Articles


李敏a,b, 刘茂华a, 王琪a, 王克让a, 李小六a   

  1. a 河北大学化学与环境科学学院 药物化学与分子诊断教育部重点实验室 河北省化学生物学重点实验室 河北保定 071002;
    b 邢台学院化学与化工学院 河北邢台 054001
  • 收稿日期:2019-08-14 修回日期:2019-09-24 发布日期:2019-10-25
  • 通讯作者: 王克让, 李小六;
  • 基金资助:

Synthesis and Glycosidase Inhibition Activity of an Amphiphilic Fatty-Deoxynojirimycin Derivative

Li Mina,b, Liu Maohuaa, Wang Qia, Wang Keranga, Li Xiaoliua   

  1. a Key Laboratory of Medicinal Chemistry and Molecular Diagnosis (Ministry of Education), Key Laboratory of Chemical Biology of Hebei Province, College of Chemistry and Environmental Science, Hebei University, Baoding, Hebei 071002;
    b College of Chemistry and Chemical Engineering, Xingtai University, Xingtai, Hebei 054001
  • Received:2019-08-14 Revised:2019-09-24 Published:2019-10-25
  • Supported by:
    Project supported by the National Natural Science Foundation of China (Nos. 21572044, 21778013), the Natural Science Foundation of Hebei Province (No. B2016201254), and the Foundation of Hebei Education Department (No. QN2018310).

An amphiphilic derivative FA-DNJ-C6 with deoxynojirimycin modification was synthesized. The self-assembly behavior of FA-DNJ-C6 was studied by a surface tension test, dynamic light scattering test (DLS) and transmission electron microscopy (TEM). FA-DNJ-C6 formed stable supramolecular self-assembly in aqueous solution. Furthermore, the glycosidase inhibition activities of FA-DNJ-C6 were studied. FA-DNJ-C6 as multivalent glycosidase inhibitor showed potent glycosidase effect against α-mannosidase with Ki value of (0.107±0.021) μmol/L, an increase of approximately 339-fold compared with the control drug of miglitol, which was due to the multivalent binding sites in α-mannosidase.

Key words: glycosidase inhibitor, self-assembly, multivalent, 1-deoxynojirimycin