Journal article

Membrane interactions and the effect of metal ions of the amyloidogenic fragment A beta(25-35) in comparison to A beta(1-42)

Tong-Lay Lau, John D Gehman, John D Wade, Keyla Perez, Colin L Masters, Kevin J Barnham, Frances Separovic

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | ELSEVIER SCIENCE BV | Published : 2007

Abstract

Abeta(1-42) peptide, found as aggregated species in Alzheimer's disease brain, is linked to the onset of Alzheimer's disease. Many reports have linked metals to inducing Abeta aggregation and amyloid plaque formation. Abeta(25-35), a fragment from the C-terminal end of Abeta(1-42), lacks the metal coordinating sites found in the full-length peptide and is neurotoxic to cortical cortex cell cultures. We report solid-state NMR studies of Abeta(25-35) in model lipid membrane systems of anionic phospholipids and cholesterol, and compare structural changes to those of Abeta(1-42). When added after vesicle formation, Abeta(25-35) was found to interact with the lipid headgroups and slightly perturb..

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