Jian Cui

Southwest Jiaotong University, Hua-yang, Sichuan, China

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Publications (3)2.27 Total impact

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    ABSTRACT: Elevated expression of forkhead/winged helix transcription factor FOXM1 are closely involved in cancer initiation, invasion and metastasis. It is a potentially suitable target for anticancer drug discovery and therapy. In this study, we investigated the expression and selection of human Foxm1c binding peptides and their inhibitions on MCF7 cancer cells. The protein of DNA binding domain of human FoxM1c(DBDFoxM1c) was expressed in prokaryotic system and then purified and later used as the target for binding peptide selection based on the phage random dodecapeptide library. The phages were enriched after four rounds of selection and 18 different peptide sequences were obtained. seven possible consensus peptide sequences WHL/Q/D/N, DL/HL/NY, SSLWN/E; HLD/YY/E; YH/LE/D/E/D; YPH/L/S and F/NY/FN/YL were identified and they were found to dock well to the 3D structure model of DBDFoxM1c by molecular docking. One representative peptide was designed and in vitro study revealed that the viability of MCF7 cancer cells could be reduced to 34.30 % at the concentration of 100 µg/ml of the peptide. In conclusion, the consensus peptide sequences identified in our study were newly reported and it is the first report of the screening of binding peptides targeting DBDFoxM1c. We expect that the results of these studies will result in future development of FoxM1c based lead peptide drug as well as the further understanding of DBDFoxM1c.
    International Journal of Peptide Research and Therapeutics 12/2014; 20(4). · 1.28 Impact Factor
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    ABSTRACT: Subtractive cell surface panning from phage random peptide library and molecular docking were used to select and find binding peptides dual-targeting MMP14 and metal ions on MG-63 cells. Phages were abundantly enriched and totally 22 different peptide sequences were obtained. We demonstrated that the affinity phage peptides were not only targeted to MMP14 but also had affinities for zinc and nickel ions. Four possible peptide consensus sequences were identified as: AHQ/ S LH/ P , L/ I / E PLL/ I , T/Q/ D ARH/ F Q, MK/ P SR. The representative peptides were found to dock well to MMP14 at the sites around aa. 120–125 which were also the catalytic region of zinc binding sites on MMP14 by MVD molecular docking. The selected monoclonal phages could efficiently bind to the MMP14 expressed MG-63 cells and this again confirmed the targeting binding of the peptides to MMP14. In vitro study revealed that the selected monoclonal phages could greatly inhibit the viability of MG-63 cells. Also, the four synthetic
    International Journal of Peptide Research and Therapeutics 03/2011; · 0.99 Impact Factor
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    ABSTRACT: Receptor structured-based virtual screening is routinely used in computer aided drug design. Membrane-type matrix metalloproteinase-1(MT1-MMP, also called MMP-14) plays a key role in tumor invasion and metastasis by degrading the extracellular matrix and activating proMMP2. The Hemopexin-like (HPX) domain of MT1-MMP is required for MT1-MMP-mediated tumor invasion and growth in three-dimension type I collagen matrix. Here, we describe the virtual screening of lead chemicals based on the HPX domain of MT1-MMP. DOCK, MVD and metaPocket were used in detecting and identifying of the potential active sites on the surface of HPX domain of MT1-MMP. DOCK and AutoDock were used for docking ligands from Specs chemical database to two potential active sites. The result indicates that the sphere cluster 3 identified by the program in DOCK, sphgen, might be a right active site used for HPX structured-based docking study. A group of chemical compounds have been identified and may be used for further study as lead molecules. Our study also provides better insight to virtual screening study based on receptor in condition of no receptor-ligand complex crystal structure is available.