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• W2022756726 abstract "Aggregation of the Aβ1–40 peptide is linked to the development of extracellular plaques characteristic of Alzheimer’s disease. While previous studies commonly show the Aβ1–40 is largely unstructured in solution, we show that Aβ1–40 can adopt a compact, partially folded structure. In this structure (PDB ID: 2LFM), the central hydrophobic region of the peptide forms a 310 helix from H13 to D23 and the N- and C-termini collapse against the helix due to the clustering of hydrophobic residues. Helical intermediates have been predicted to be crucial on-pathway intermediates in amyloid fibrillogenesis, and the structure presented here presents a new target for investigation of early events in Aβ1–40 fibrillogenesis." @default.
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• W2022756726 date "2011-07-01" @default.
• W2022756726 modified "2023-09-29" @default.
• W2022756726 title "A partially folded structure of amyloid-beta(1–40) in an aqueous environment" @default.
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• W2022756726 doi "https://doi.org/10.1016/j.bbrc.2011.06.133" @default.
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