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ToF-SIMS Analysis of Amyloid Beta Aggregation on Different Lipid Membranes

ToF-SIMS Analysis of Amyloid Beta Aggregation on Different Lipid Membranes

Yuta Yokoyama, Satoka Aoyagi, Toshinori Shimanouchi, Miki Iwamura, Hideo Iwai

Biointerphases. 2016 Jun 28;11(2):02A314.

PMID: 26822505

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP7073612	Cholesterol β-D-glucoside		7073-61-2	Price

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