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Selected Publication:

Song, H; Sinner, EK; Knoll, W.
(2007): Peptid-tethered bilayer lipid membranes and their interaction with Amyloid beta-peptide.
Biointerphases. 2007; 2(4):151-158 FullText FullText_BOKU

Abstract:
The Amyloid peptide (A beta), a normal constituent of neuronal and non-neuronal cells, has been shown to be a major component of the extracellular plaque of Alzheimer disease (AD). The interaction of A beta peptides with the lipid matrix of neuronal cell membranes plays an important role in the pathogenesis of AD. In this study, we have developed peptide-tethered artificial lipid membranes by the Langmuir-Blodgett and Langmuir-Schaefer methods. Anti-A beta 40-mAb labeled with a fluorophore was used to probe A beta 40 binding to these model membranes. Systematic studies on the antibody or A beta-membrane interactions were carried out by surface plasmon field-enhanced fluorescence spectroscopy. It was found that the A beta adsorption is critically depending on the lipid composition of the membranes, with A beta specifically binding to membranes containing sphingomyelin. Further, this preferential adsorption was markedly amplified by the addition of sterols (cholesterol or 25- OH- Chol). (c) 2007 American Vacuum Society.
Authors BOKU Wien:
Ehmoser Eva-Kathrin



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