Surface chemistry of lipid raft and amyloid Aβ (1-40) Langmuir monolayer

Lipid rafts being rich in cholesterol and sphingolipids are considered to provide ordered lipid environment in the neuronal membranes, where it is hypothesized that the cleavage of amyloid precursor protein (APP) to Aβ (1-40) and Aβ (1-42) takes place. It is highly likely that the interaction of lipid raft components like cholesterol, sphingomylein or GM1 leads to nucleation of Aβ and results in aggregation or accumulation of amyloid plaques. One has investigated surface pressure–area isotherms of the lipid raft and Aβ (1-40) Langmuir monolayer. The compression–decompression cycles and the stability of the lipid raft Langmuir monolayer are crucial parameters for the investigation of interaction of Aβ (1-40) with the lipid raft Langmuir monolayer. It was revealed that GM1 provides instability to the lipid raft Langmuir monolayer. Adsorption of Aβ (1-40) onto the lipid raft Langmuir monolayer containing neutral (POPC) or negatively charged phospholipid (DPPG) was examined. The adsorption isotherms revealed that the concentration of cholesterol was important for adsorption of Aβ (1-40) onto the lipid raft Langmuir monolayer containing POPC whereas for the lipid raft Langmuir monolayer containing DPPG:cholesterol or GM1 did not play any role. In situ UV–vis absorption spectroscopy supported the interpretation of results for the adsorption isotherms.

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► Surface chemistry and in situ spectroscopy of lipid raft and Aβ (1-40) Langmuir monolayer were studied.
► It was revealed that the lipid raft Langmuir monolayer was unstable at the air–water interface.
► Adsorption of Aβ (1-40) on the lipid raft Langmuir monolayer containing POPC as one of the component was cholesterol dependent.
► Adsorption of Aβ (1-40) was independent of cholesterol concentration in case of lipid raft Langmuir monolayer containing negatively charged phospholipid DPPG as one of the components.