To study the interaction between melittin peptides and lipid bilayer we performed: coarse grained Simulations on systems containing melittin interacting with a :bilayer containing zwitterionic dipalmitoylphosphatidylchnline (DPpc) and anionic palmitoyloleoylphosphatidylglycerol (POPG) phospholipids in a 7:3 ratio. Eight different systems were considered: :four at low and four at high peptide to lipid (P/L), ratios. In. case of low P/L ratio we did not observe any pore Creation in the bilayer. In two out of four of the simulations with the high P/L ratio, appearance of transient pores in the bilayer was observed. These pores were created due to an assembly of 3-5 melittin peptides. Not all of the peptides in the pores were in a transmembrane conformation; many of them had their termini. residues anchored to the same leaflet, and these peptides assumed bent, U-shaped, conformations. We propose that when an assembly of melittin peptides creates pores, such an assembly acts as a "wedge" that splits the bilayer. To get a more detailed description of melittin on the bilayer surface and in transient pores, we performed coarse-grained to united-atom scale transformations and after that performed 50 ns molecular dynamics Simulations using the united atom description of the systems. While these simulations did not show much of the change in the pore structure during the 50 ns time interval, they clearly showed the presence of water in the transient pores. The appearance of transient pores together with the translocation of peptides across the membranes is consistent with the mechanism proposed to explain graded dye leakage from large vesicles in the presence of melittin.