The transition of alpha-helical or unfolded peptides and proteins to beta-sheets and the subsequent amyloid formation are characteristic for neurodegenerative diseases like Alzheimer's or Parkinson's disease. The interactions of amyloidogenic peptides with surfaces such as biological membranes are considered to play an important role regarding the onset of secondary structure changes. In our project, we used a peptide designed to have specific secondary structure propensities in order to investigate the driving forces and conditions which lead to the beta-sheet formation. The model peptide is able to adopt the coiled coil conformation, alpha-helical peptide strands that wind around each other in a superhelical structure. In addition to building principles stabilizing this alpha-helical conformation it also has beta-sheet stabilizing features. We focused on the interactions of the peptide with the hydrophobic air-water interface. Infrared reflection absorption spectroscopy was used as a surface sensitive method and complemented with grazing incidence X-ray diffraction and reflectivity. Furthermore, the model peptide provides metal binding sites. The binding of transition metal ions leads to a local preference of certain secondary structure elements, depending on the metal ion and the geometry of metal ion binding sites. The interplay and competition of the two trigger mechanisms (1) interaction with surfaces and (2) metal ion complexation were investigated. We found that the secondary structure of the peptide strongly depends on the interactions with the hydrophobic air-water interface and the orientation imposed by it. The metal ions Zn(2+) and Cu(2+) were used for complexation. The structure of the peptide surface layer differs according to the bound metal ion.