While the majority of known antimicrobial peptides are cationic, a small number consist of short Asp-rich sequences that are anionic. These require metal ions to become biologically active. Here, we report the study of the zinc complexes of the peptide GADDDDD (GAD5), an antimicrobial peptide. Using a combination of dynamic light scattering (DLS), ζ-potential, infrared, Raman, thermogravimetric analysis (TGA), differential scanning calorimetry (DSC), and scanning electron microscopy (SEM), we find that adding zinc ions to GAD5 forces it into a compact structure. Higher amounts of zinc ions favor a larger structure, possibly a dimer. SEM images show that zinc ions reduce the size of the fibrillar structures of GAD5. TGA curves show that the addition of zinc ions increases the thermal stability of the structure of the peptide. TGA and DSC indicate that the association of GAD5 with a zwitterionic phospholipid in the presence of zinc ions is the most stable. The stability of that complex is due to the presence of a sharp endothermic peak in the 200-300 °C range, suggesting the presence of interlamellar water that is essential to the stabilization of the structure. These results indicate that the Zn-GAD5 complex prefers the bacteria-mimicking neutral (zwitterionic) membranes. In the presence of negatively charged phospholipids, the complex remains unordered and unstable. In terms of mechanism of action, the Zn-GAD5 complex promotes a possible endocytic uptake with respect to neutral (zwitterionic) membranes while promoting membrane disruption by forming pores with respect to negatively charged phospholipids.