Cationic antimicrobial peptides play a key role in the first line of defense against invading pathogens. Many studies on these peptides objectify the substitution of classic antibiotics because of the increasing resistance of the pathogens. The antimicrobial peptide indolicidin (ILPWKWPWWPWRR-NH₂) isolated from cytoplasmatic granule of bovine neutrophils has a broad spectrum of antimicrobial activity against pathogens being cytotoxic to rat and human T-lymphocytes and lyses erythrocytes. The antimicrobial and cytotoxic activities are correlated with the lipid charges of the membranes that are frequently negatively charged in the bacteria. On the other hand, many of the mammalian cells lipids are neutral. The objective of the present study is to help to clarify how the cytotoxic activity can be correlated with the indolicidin/DPC micelle behavior. The investigation will be made by molecular dynamics simulation carried out using the GROMACS package (version 3.2) with the GROMACS force field and SPC model for water at 300 K and 1 bar in the NPT ensemble applying the Berendsen's algorithms for the p and T couplings. The simulation was initiated inserting the peptide in the center of the micelle. The root mean square deviation for backbone atoms increases rapidly to 1.5 Å after 0.3 ns,  2  Å at 1.6 ns and then increases smoothly with a  stabilization near 2.5  Å until 20 ns . The peptide/micelle energy interaction (initially in -1015 kJ.mol^-1) stabilizes around -1800 kJ.mol^-1. The results indicate that the micelle environment stabilizes the peptide structure to the same structure observed by NMR experiments in DPC environment.