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| Home > Publications database > Disorder-to-order transition of the amyloid-β peptide upon lipid binding |
| Journal Article | FZJ-2021-04247 |
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2022
Elsevier Science
Amsterdam [u.a.]
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Please use a persistent id in citations: http://hdl.handle.net/2128/33549 doi:10.1016/j.bpc.2021.106700
Abstract: 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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