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- W2146914013 abstract "We investigate the role played by membrane composition on the interaction and self-assembly of β-amyloid peptide (AβP1–40) during pore formation in planar lipid membranes (PLMs). Incorporation studies showed that AβP does not interact with zwitterionic membranes made up of phosphatidylcholine, whereas the addition of cholesterol or ergosterol to the membranes leads to channel formation. Among the PLMs used, a higher propensity of AβP to form channels at low applied potential (±20 mV) was observed in 7-dehydrocholesterol and in oxidized cholesterol PLMs. These channels present long lifetimes, high-occurrence frequencies, and are voltage dependent. In particular, the AβP channel in oxidized cholesterol showed anion selectivity. Thus cholesterol (and sterols in general) could be considered as targets for AβP, which prevents the fibrillation process by increasing incorporation into membranes. Furthermore, by switching the channel selectivity versus anions, cholesterol helps to reduce the imbalance of the cellular ions, calcium included, induced by membrane depolarization, which could be one of the factors responsible for cytotoxicity in Alzheimer’s disease." @default.
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- W2146914013 date "2004-04-01" @default.
- W2146914013 modified "2023-10-02" @default.
- W2146914013 title "Effect of Sterols on β-Amyloid Peptide (AβP 1–40) Channel Formation and their Properties in Planar Lipid Membranes" @default.
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- W2146914013 doi "https://doi.org/10.1016/s0006-3495(04)74281-2" @default.
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