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- W3019632310 abstract "Among the family of Aβ peptides, pyroglutamate-modified Aβ (AβₚE) peptides are particularly associated with cytotoxicity in Alzheimer’s disease (AD). They represent the dominant fraction of Aβ oligomers in the brains of AD patients, but their accumulation in the brains of elderly individuals with normal cognition is significantly lower. Accumulation of AβₚE plaques precedes the formation of plaques of full-length Aβ (Aβ₁₋₄₀/₄₂). Most of these properties appear to be associated with the higher hydrophobicity of AβₚE as well as an increased resistance to enzymatic degradation. However, the important question of whether AβₚE peptides induce pore activity in lipid membranes and their potential toxicity compared with other Aβ pores is still open. Here we examine the activity of AβₚE pores in anionic membranes using planar bilayer electrical recording and provide their structures using molecular dynamics simulations. We find that AβₚE pores spontaneously induce ionic current across the membrane and have some similar properties to the other previously studied pores of the Aβ family. However, there are also some significant differences. The onset of AβₚE₃₋₄₂ pore activity is generally delayed compared with Aβ₁₋₄₂ pores. However, once formed, AβₚE₃₋₄₂ pores produce increased ion permeability of the membrane, as indicated by a greater occurrence of higher conductance electrical events. Structurally, the lactam ring of AβₚE peptides induces a change in the conformation of the N-terminal strands of the AβₚE₃₋₄₂ pores. While the N-termini of wild-type Aβ₁–₄₂ peptides normally reside in the bulk water region, the N-termini of AβₚE₃₋₄₂ peptides tend to reside in the hydrophobic lipid core. These studies provide a first step to an understanding of the enhanced toxicity attributed to AβₚE peptides." @default.
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- W3019632310 date "2014-01-01" @default.
- W3019632310 modified "2023-09-23" @default.
- W3019632310 title "Activity and Architecture of Pyroglutamate-Modified Amyloid-β (AβpE3-42) Pores" @default.
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