Interaction of the beta-amyloid peptide with lipid bilayers: the role of omega-3 fatty acids.
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 Aâ–membrane 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.
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PADUANO Luigi; BARKER Robert; LUCHINI Alessandra; MANGIAPIA Gaetano; SANTAGATA Rosa Alba and VITIELLO Giuseppe. (2013). Interaction of the beta-amyloid peptide with lipid bilayers: the role of omega-3 fatty acids.. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-668
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