The amyloid beta-protein (Abeta) constitutes the major peptide component of the amyloid plaque deposits of Alzheimer's disease in humans. The Abeta changes from a nonpathogenic to a pathogenic conformation resulting in self-aggregation and deposition of the peptide. It has been established that denaturing factors (such as the interaction with membranes) are involved in the structural transition. This work is aimed at determining the effect of hydrophobic Teflon on the conformation of the Abeta (1-40). Prior to adsorption, the secondary structure and self-aggregation state of the Abeta in solution were established as a function of pH. Three different species coexist: unordered monomers/dimers, small oligomers in mainly a regular beta-sheet structure, and bigger aggregates having a twisted beta-sheet conformation. Transferring the A from the solution to the Teflon surface strongly promotes alpha-helix formation. Furthermore, increasing the degree of coverage of the Teflon by the Abeta protein leads to a conformational change toward a more enriched beta-sheet structure.