Jian Cui

Southwest Jiaotong University, Hua-yang, Sichuan, China

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Publications (5)2.69 Total impact

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    ABSTRACT: Membrane type-1 matrix metalloproteinase (MT1-MMP; also known as MMP14) is a key enzyme involved in tumor invasion and metastasis, and is a potential target for drug discovery for cancer therapy. However, till now there is no MT1-MMP- or MMP-based anticancer drugs in the market mainly because of the high conservation of the MMP family and also because there is no elucidated crystal structure for the mature MT1-MMP. The modeling of the three-dimensional structure of mature MT1-MMP and the finding of MT1-MMP targeted peptides by virtual screening are highly desired. In this study, the three-dimensional structure of mature MT1-MMP is constructed by homology and de novo modeling and later rationalized and optimized by molecular dynamics simulations. An antisense peptide library was constructed against the divergent sense peptide DEGTEEET in the specific region of MT1-MMP, which was found by multiple alignment of the whole MMP family. The antisense peptide library was virtually screened against the constructed three-dimensional model of MT1-MMP. The top 20 novel peptides were further studied, which were found well docked with MT1-MMP at the region of DEGTEEET, again confirming their specific binding to MT1-MMP. Preliminary study of one of the top-ranked peptide SFLLSPFV showed that it could inhibit the viabilities of MG63 and MDA-MB-231 tumor cells. We thus not only successfully modeled the three-dimensional structure of mature MT1-MMP but also provided a new way for the finding of peptide candidates targeting MT1-MMP based on antisense peptide library. © 2015 Korean Chemical Society & Wiley-VCH Verlag GmbH & Co. KGaA.
    No preview · Article · Sep 2015 · Bulletin of the Korean Chemical Society
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    ABSTRACT: Hericium erinaceus possesses multiple medicinal values. To date, however, there have been few studies of the systemic screening of H. erinaceus strains, and the neuroprotective effects of H. erinaceus prepared from homogenized, fresh fruiting bodies are not fully understood. In this study, 4 random primers were selected and used in random amplified polymorphic DNA (RAPD) polymerase chain reaction (PCR) to screen and evaluate the genetic diversity of 19 commercial strains of H. erinaceus from different localities in China. A total of 66 bands were obtained, and the percentage of polymorphic loci reached 80.30%. Five dendrograms were constructed based on RAPD by Jaccard cluster and within-group linkage analysis. Primer S20 as well as all 4 primers had great potential as specific primers for RAPD-PCR molecular identification and differentiation of H. erinaceus strains. Based on the results of submerged culture and fruiting body cultivation, strains HT-N, HT-J1, HT-C, and HT-M were identified as superior among the 19 H. erinaceus strains. Further study showed that the oral preparation of homogenized, fresh fruiting bodies of H. erinaceus could attenuate the Aβ25-35-triggered damage in PC12 cells by significantly increasing cell viability and by decreasing the release of lactate dehydrogenase. In conclusion, RAPD-PCR combined with liquid and solid cultures can be used well in the screening and identification of H. erinaceus strains, and products prepared from homogenized, fresh fruiting bodies of H. erinaceus had neuroprotective effects on PC12 cells.
    No preview · Article · May 2015
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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.
    No preview · Article · Dec 2014 · International Journal of Peptide Research and Therapeutics
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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
    No preview · Article · Mar 2011 · International Journal of Peptide Research and Therapeutics
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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.
    No preview · Article · Jan 2011