Utilization of Recombinant Mojastin Peptides for Cell Migration Inhibition of SK-Mel-28 Cells

This study utilizes disintegrins possessing an Arginine-Glycine-Aspartic Acid (RGD) motif in an attempt to inhibit cell migration in SK-Mel-28 cells. Disintegrins are non-enzymatic, low molecular weight peptides with a cysteine-rich portion and an integrin binding loop. Integrins are heterodimeric transmembrane receptors composed of alpha and beta subunits. When a disintegrin binds to an integrin, the integrin can emit intracellular signals that can cause a cell to migrate. The two successive amino acids that are carboxyl to the RGD complex are a topic of interest because they have been shown to alter the function of the disintegrin. Our hypothesis is that r-Moj peptides containing different amino acids carboxyl of the RGD will inhibit cell migration of SK-Mel-28.  Cell migration was tested in triplicates using the wound healing assay by Platypus Technology.  The SK-Mel-28 cells in a cell migration assay were treated with 3 µM of six isolated recombinant mojastin (r-Moj) mutants.  These were r-Moj-DA, r-Moj-NM, r-Moj-MN, r-Moj-WL, r-Moj-WM, and r-Moj-WP.  The results after 24 hrs of incubation indicate that all tested r-Moj peptides, except for r-Moj-WL, inhibited cell migration significantly (p<0.05). We will extend our cell migration inhibition analysis to 48 hrs after treatment.  Thus, our data supports our hypothesis.  This research was funded by NSF-REU grant DBI 1004350.