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001     902425
005     20230224084259.0
024 7 _ |a 10.1016/j.bpc.2021.106700
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024 7 _ |a 0301-4622
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024 7 _ |a 1873-4200
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024 7 _ |a 2128/33549
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037 _ _ |a FZJ-2021-04247
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100 1 _ |a Fatafta, Hebah
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245 _ _ |a Disorder-to-order transition of the amyloid-β peptide upon lipid binding
260 _ _ |a Amsterdam [u.a.]
|c 2022
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520 _ _ |a There is mounting evidence that Alzheimer's disease progression and severity are linked to neuronal membrane damage caused by aggregates of the amyloid- (A) peptide. However, the detailed mechanism behind the membrane damage is not well understood yet. Recently, the lipid-chaperone hypothesis has been put forward, based on which the formation of complexes between A and free lipids enables an easy insertion of A into membranes. In order to test this hypothesis, we performed numerous all-atom molecular dynamics simulations. We studied the complex formation between individual lipids, considering both POPC and DPPC, and A and examined whether the resulting complexes would be able to insert into lipid membranes. Complex formation at a one-to-one ratio was readily observed, yet with minimal effects on A's characteristics. Most importantly, the peptide remains largely disordered in 1:1 complexes, and the complex does not insert into the membrane; instead, it is adsorbed to the membrane surface. The results change considerably once A forms a complex with a POPC cluster composed of three lipid molecules. The hydrophobic interactions between A and the lipid tails cause the peptide to fold into either a helical or a -sheet structure. These observations provide atomic insight into the disorder-to-order transition that is needed for membrane insertion or amyloid aggregation to proceed.
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700 1 _ |a Kav, Batuhan
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700 1 _ |a Bundschuh, Bastian F.
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700 1 _ |a Loschwitz, Jennifer
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700 1 _ |a Strodel, Birgit
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|e Corresponding author
773 _ _ |a 10.1016/j.bpc.2021.106700
|g Vol. 280, p. 106700 -
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|t Biophysical chemistry
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856 4 _ |u https://juser.fz-juelich.de/record/902425/files/Fatafta-BiophysChem-2022_Disorder-to-order%20transition%20of%20the%20amyloid-%C3%9F%20peptide%20upon%20lipid%20binding-1.pdf
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