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- W1978334807 abstract "Fluorescence Resonance Energy Transfer (FRET) was used to study protein structures within soluble oligomer intermediates of amyloid and non-amyloid aggregates. Three protein aggregation systems were studied using fluorescence donor and acceptor near the N and C terminus:(1) Alzheimer's Aβ1-40 peptide.(2) 20-residue polyglutamine K2Q16K2.(3) 20-residue polyglutamic acid E20. (non-amyloid)The aggregation of each peptide showed different conformational changes: Aβ1-40 partially compacted into a structure consistent with solid-state NMR structures, K2Q16K2 extended to form β-sheets, and E20 compacted heavily into β-hairpins. However, based on donor-acceptor distances, soluble oligomers conformations of all three peptides show a remarkable degree of similarity to their monomeric precursors, albeit with a slightly expanded conformation for Aβ1-40 and E20. These findings support assembly models of small soluble oligomers which largely consist of monomer-like structures, with some increase in α-helical content for Aβ1-40. These donor-acceptor distances are used to directly assess the accuracy of different molecular dynamics force fields in the study of these soluble oligomers." @default.
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- W1978334807 date "2009-02-01" @default.
- W1978334807 modified "2023-09-27" @default.
- W1978334807 title "Amyloid Peptide Conformations In Soluble Oligomers" @default.
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- W1978334807 doi "https://doi.org/10.1016/j.bpj.2008.12.359" @default.
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