Amyloid beta (Aβ) peptides are considered to be strongly related to Alzheimer’s disease. Aβ peptides form a β-sheet structure on hard lipid membranes and it would aggregate to form amyloid fibrils, which are toxic to cells. However, the aggregation mechanism of Aβ is not fully understood. To evaluate the influence of the lipid membrane condition for Aβ aggregation, the adsorption forms of Aβ (1–40) on mixture membranes of lipid 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and cholesterol β-D-glucoside (β-CG) were investigated by time-of-flight secondary ion mass spectrometry. As a result, Aβ adsorbed along the localized DMPC lipid on the mixture lipid membranes, whereas it was adsorbed homogeneously on the pure DMPC and β-CG membranes. Moreover, amino acid fragments that mainly existed in the n-terminal of Aβ (1–40) peptide were strongly detected on the localized DMPC region. These results suggested that the Aβ was adsorbed along the localized DMPC lipid with a characteristic orientation. These findings suggest that the hardness of the membrane is very sensitive to coexisting materials and that surface hardness is important for aggregation of Aβ.
|Number of pages||6|
|Publication status||Published - Jun 1 2016|
ASJC Scopus subject areas
- Materials Science(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Physics and Astronomy(all)