This work describes the synthesis and characterization of copper (II) and zinc (II) complexes, with dipeptides in solid state. The dipeptides involved were: glycyl-glycine, glycyl-valine, methionyl-methionine, methionyl-glycine and cysteinyl-glycine, whose aminoacids take part in some proteins involved in neurodegeneration processes, more specifically in Alzheimer’s disease. Although the mechanisms that trigger this pathology are still not totally clear, it is known that metallic ions, such as copper (II) and zinc (II) interact with the beta-amyloid peptide. It seems that such interactions favor the formation of solid proteic aggregates of this peptide, observed in the brains of patients with Alzheimer’s disease. Thus, the obtaining and study of simple models in the solid state, synthesized in similar conditions to the biological medium, may allow a better understanding of the possible interactions of such metals in this proteic site. The compounds obtained were characterized using the following techniques: elemental analysis, atomic absorption, infrared spectroscopy, Raman spectroscopy, ultraviolet-visible spectroscopy, thermogravimetry, EPR (for the copper complexes) and conductivimetry. For the zinc complexes, quantum-mechanical theoretical calculations were performed to obtain geometrical parameters and infrared spectra. The analysis of the compounds showed that the copper and zinc complexes with dipeptides are coordinated through oxygen and nitrogen atoms. In complexes of dipeptides containing sulfur, coordination trough the sulfur atom occurs too (copper with methionyl-methionine and methionyl-glycine and zinc with cysteinyl-glycine). The compounds obtained for both metals at the metal-ligand ratio (1:1) behave differently from those studied in solution e those obtained in the metal-ligand ratio (1:2) show similar behavior of metal complexes with aminoacids.