beta-Amyloid (1-42), rat

Abeta 1-42 induces a strong membrane destabilization in giant unilamellar vesicles composed of palmitoyloleoyl-phosphatidylcholine, sphingomyelin, and cholesterol, lowering the critical tension of vesicle rupture. Additionally, Abeta 1-42 triggers the induction of sequential leakage of low- and high-molecular-weight markers trapped inside the giant unilamellar vesicles, but preserving the vesicle shape. The Abeta 1-42 sequence confers particular molecular properties to the peptide that, in turn, influence supramolecular properties associated with membranes that may result in toxicity,including: 1) the ability of the peptide to strongly associate with the membrane; 2) a reduction of lateral membrane cohesive forces; and 3) a capacity to break the transbilayer gradient and puncture sealed vesicles.