The morphological hallmarks found in the brains of AD patients are extracellular senile plaques, composed of insoluble beta-amyloid peptide (Abeta) fibrillar aggregates. Abeta peptides derive from the proteolytic cleavage of the trans-membrane amyloid precursor protein and the predominant form is Abeta(1-42). Once Abeta is produced, it can be released as a soluble, unfolded unimer into the extracellular environment and be removed or it could accumulate, and eventually self-aggregate in ordered fibrils, undergoing a conformational transition to â-sheet structure. Many studies suggest that the membrane surface may act as a two-dimensional template for fibril nucleation seeds. A particular interest has been developed in Aâmembrane interactions in order to elucidate the molecular mechanisms of the Aâ-induced cellular dysfunctions underlying the pathogenesis of AD. At the same time, a strong interest is addressed to define strategies for AD prevention and therapy. One of these is related to the dietary components, like omega-3 fatty acids, that appear to play an important role in preventing the disease, possibly changing the physic-chemical properties of the membrane.