[show abstract]
[hide abstract]
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 01/2011; · 0.99 Impact Factor
