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- W2071490247 abstract "Aβ (16–35) is the hydrophobic central core of β-amyloid peptide, the main component of plaques found in the brain tissue of Alzheimer's disease patients. Depending on the conditions present, β-amyloid peptides undergo a conformational transition from random coil or α-helical monomers, to highly toxic β-sheet oligomers and aggregate fibrils. The behavior of β-amyloid peptide at plasma membrane level has been extensively investigated, and membrane charge has been proved to be a key factor modulating its conformational properties. In the present work we probed the conformational behavior of Aβ (16–35) in response to negative charge modifications of the micelle surface. CD and NMR conformational analyses were performed in negatively charged pure SDS micelles and in zwitterionic DPC micelles “doped” with small amounts of SDS. To analyze the tendency of Aβ (16–35) to interact with these micellar systems, we performed EPR experiments on three spin-labeled analogues of Aβ (16–35), bearing the methyl 3-(2,2,5,5-tetramethyl-1-oxypyrrolinyl) methanethiolsulfonate spin label at the N-terminus, in the middle of the sequence and at the C-terminus, respectively. Our conformational data show that, by varying the negative charge of the membrane, Aβ (16–35) undergoes a conformational transition from a soluble helical–kink–helical structure, to a U-turn shaped conformation that resembles protofibril models." @default.
- W2071490247 created "2016-06-24" @default.
- W2071490247 creator A5015817418 @default.
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- W2071490247 creator A5026034661 @default.
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- W2071490247 creator A5030599017 @default.
- W2071490247 creator A5040940946 @default.
- W2071490247 creator A5058519678 @default.
- W2071490247 date "2010-03-01" @default.
- W2071490247 modified "2023-10-17" @default.
- W2071490247 title "Membrane charge dependent states of the β-amyloid fragment Aβ (16–35) with differently charged micelle aggregates" @default.
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